Structure of N-acetylneuraminic acid phosphatase: Difference between revisions

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__TOC__
__TOC__


===CHAIN SEQUENCE===
===Chain Sequence===
MGSDKIHHHHHHMGLSRVRAVFFDLDNTLIDTAGASRRGMLEVIKLLQSKYHYKEEAEIICDKVQVKLSKECFHPYSTCI
MGSDKIHHHHHHMGLSRVRAVFFDLDNTLIDTAGASRRGMLEVIKLLQSKYHYKEEAEIICDKVQVKLSKECFHPYSTCI
TDVRTSHWEEAIQETKGGADNRKLAEECYFLWKSTRLQHMILADDVKAMLTELRKEVRLLLLTNGDRQTQREKIEACACQ
TDVRTSHWEEAIQETKGGADNRKLAEECYFLWKSTRLQHMILADDVKAMLTELRKEVRLLLLTNGDRQTQREKIEACACQ
Line 8: Line 8:


[[Image:2gfh asym r 250.jpg|thumb|structure 18|left]]
[[Image:2gfh asym r 250.jpg|thumb|structure 18|left]]
[[Image:Interpro1.JPG|interpro|left]]




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===EXTERNAL LINK===
[http://www.ebi.ac.uk/msd-srv/msdlite/atlas/summary/2gfh.html 1. EBI Mcromolecular Structure Database]






===DALI SEARCH RESULTS===
===DALI Search Results===


  SUMMARY: PDB/chain identifiers and structural alignment statistics
  SUMMARY: PDB/chain identifiers and structural alignment statistics
Line 98: Line 126:
  29: 3033-A 1mh9-A  9.2  3.2  146  194  15      0      0    15 S    HYDROLASE        deoxyribonucleotidase (mitochondrial  5'(3')-
  29: 3033-A 1mh9-A  9.2  3.2  146  194  15      0      0    15 S    HYDROLASE        deoxyribonucleotidase (mitochondrial  5'(3')-


===Alignments of top-scoring domains===
===Surface properties===
 
[[Image:Surface properties.JPG]]
 
===From PDB===
Chemical component identifier would be     
 
PO4    PHOSPHATE ION
         
NA    SODIUM ION
         
EDO    1,2-ETHANEDIOL
 
CL    CHLORIDE ION
 
Closely related to 2HO4,PO4    PHOSPHATE ION found.
 
Cloesly related to 2HX1,CL    Chloride Ion, EDO  1 2 Ethanediol  found. 
 
'''2GFH'''
http://www.rcsb.org/pdb/explore/biologyAndChemistry.do?structureId=2GFH
 
'''2HX1'''
http://www.rcsb.org/pdb/explore/biologyAndChemistry.do?structureId=2HX1
 
'''1FEZ'''
http://www.rcsb.org/pdb/explore/biologyAndChemistry.do?structureId=1FEZ
 
'''2HO4'''
http://www.rcsb.org/pdb/explore/biologyAndChemistry.do?structureId=2HO4
 
===Pubmed===
 
The identity of Asp12 as the active-site nucleophile was further evidenced by the observed removal of catalytic activity resulting from Asp12Ala substitution
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=10956028
 
 
===Pfarm classification===
PFAM Accession:PF00702
 
PFAM ID:hydrolase
 
http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00702
 
===CE===
 
'''2GFH''' USR1:A(size=260) vs '''1FEZ''' USR2:A(size=256)
Structure Alignment
 
'''2GFH'''  USR1:A - MOL_ID: 1; MOLECULE: HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN CONTAINING 4; CHAIN: A; ENGINEERED: YES
 
'''1FEZ'''  USR2:A - MOL_ID: 1; MOLECULE: PHOSPHONOACETALDEHYDE HYDROLASE; CHAIN: A, B, C, D; ENGINEERED: YES
 
 
  USR1:A  17/6    RVRAVFFDLDNTLID-TAGASRRGMLEVIKLLQSKYHYKEEAEIICDKVQVKLSKECFHP
  USR2:A    1/6    KIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRG--------VAITAEEARKPMGLL----
  USR1:A  76/#12  YSTCITDVRTSHWEEA--IQETKG---GADN--RKLAEECYFLWKST--RLQHMILADDV
  USR2:A  49/54    -----KIDHVRALTEMPRIASEWNRVFRQLPTEADIQEMYEEFEEILFAILPRYASPINA
  USR1:A  127/116  KAMLTELRK--EVRLLLLTNGDRQTQREKIEACACQ-----SYFDAIVIGGEQKEEKPAP
  USR2:A  104/109  VKEVIASLRERGIKIGSTTG----YTREMMDIVAKEAALQGYKPDFLVTPDDVPAGRPYP
  USR1:A  180/169  SIFYHCCDLLGVQP-GDCVMVGDTLETDIQGGLNAGLKATVWINK---------------
  USR2:A  160/165  WMCYKNAMELGVYPMNHMIKVGDTVSDMKEGRNAGM--WTVGVILGSSELGLTEEEVENM
  USR1:A  224/213  --------SGR-VPLTSSPMPHYMVSSVLELPALLQSI
  USR2:A  218/223  DSVELREKIEVVRNRFVENGAHFTIETMQELESVMEHI
 
'''2gfh''' USR1:A - MOL_ID: 1; MOLECULE: HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN CONTAINING 4; CHAIN: A; ENGINEERED: YES
 
'''2hx1''' USR2:A - MOL_ID: 1; MOLECULE: PREDICTED SUGAR PHOSPHATASES OF THE HAD SUPERFAMILY; CHAIN: A, B, C, D; ENGINEERED: YES
 
 
  USR1:A  65/54    QVKLSKECFHPYST------------------------------CITDVRTSHWEEAIQE
  USR2:A  24/24    VLKTYNGL------LPGIENTFDYLKAQGQDYYIVTNDASRSPEQLADSYHKL-------
  USR1:A  95/84    TKGGADNRKLAEECYFLWKSTRLQHM---ILADDVKAMLTELRKEVRLLLLTNGDRQTQR
  USR2:A  71/71    ----------GLFSI-TADKIISSGXITKEYIDLKVDGG-------IVAYLG------TA
  USR1:A  152/141  EKIEACACQSYFDAIV-----------------IGGEQKEEKPAPSIFYHCCDLLGVQPG
  USR2:A  107/107  NSANY-LVSDGIKXLPVSAIDDSNIGEVNALVLLDDEGF------NWFHDLNKTVNLLRK
  USR1:A  195/184  DC-VMVGDTL---------------ETDIQGGLNAGLKATVWI
  USR2:A  160/160  RTIPAIVANTDNTYPLTKTDVAIAIGGVATXIES-ILGRRFIR
 
'''2gfh''' USR1:A - MOL_ID: 1; MOLECULE: HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN CONTAINING 4; CHAIN: A; ENGINEERED: YES
 
'''2ho4''' USR2:A - MOL_ID: 1; MOLECULE: HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN CONTAINING 2; CHAIN: A, B; ENGINEERED: YES
 


Model:Hydrolase
  USR1:A  122/111  LADDVKAMLTELRKEV--RLLLLTNGDRQTQREKIEACACQSYFD---------AIVIGG
  USR2:A  71/72    EIFTSLTAARNLIEQKQVRPXLLLD-----------DRALPEFTGVQTQDPNAVVIGLAP
  USR1:A  171/160  EQKEEKPAPSIFYHCCDLLGVQPGDCVMVGD-------------TLETDIQGGLNAGLKA
  USR2:A  120/121  EH----FHYQLLNQAFRLLLDG--APLIAIHKARYYKRKDGLALGPGPFVTALEYATDTK
  USR1:A  218/207  TVWINKSGRVPLTSSPMPHYMVSSVLELP
  USR2:A  174/175  AXV--------------------VGKPEK
 
[[Image:2gfh and 2hx1.JPG]]
 
2gfh vs 2hx1 Rmsd = 5.6Å Z-Score = 3.1
Sequence identity = 6.2%
Aligned/gap positions = 112/111
 
 
[[Image:2gfh and 1fez.JPG]]
 
2gfh vs 1fez Rmsd = 4.4Å Z-Score = 5.5
Sequence identity = 17.4%
Aligned/gap positions = 213/65
 
 
[[Image:2gfh and 2ho4.JPG]]
 
2gfh vs 2ho4 Rmsd = 5.0Å Z-Score = 3.3
Sequence identity = 11.4%
Aligned/gap positions = 88/61
 
===ProFunc===
 
http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/profunc/GetResults.pl?source=profunc&user_id=bb32&code=143144
 
[[Image:Conserved.JPG]]
 
Diagram showing the conserved region ASN15 , Thr16, Leu17 with EDO4 molecule in grey and PO4 in yellow.
 
[[Image:Po4 ligand.JPG]]
 
IMPORTANT!!! This is involved in the function. Most likely a phosphatase.
 
[[Image:Edo4 ligand.JPG]]
 
Most likely an antifreezer.
 
[[Image:Clefts.JPG]]
 
Possible binding sites. Results shows 2 ligands PO4 and EDO4
 
===Pfam 21.0 (Janelia Farm)Alignments of top-scoring domains===
 
{| border="1" cellpadding="15" cellspacing="0"
|+'''Table of functions'''
|Model
Hydrolase
|                                             
|                                             
Seq-from:18
Seq-from:18
Line 138: Line 300:
                   + +++ +  +AG+++++++n +   
                   + +++ +  +AG+++++++n +   
       query  203 LETDIQGGLnAGLkATVWINKS    224
       query  203 LETDIQGGLnAGLkATVWINKS    224
|-
|}
===External Link===
[http://www.ebi.ac.uk/msd-srv/msdlite/atlas/summary/2gfh.html 1. EBI Mcromolecular Structure Database]
[http://www.ebi.ac.uk/cgi-bin/iprscan/iprscan?tool=iprscan&jobid=iprscan-20070515-06405113 2. InterProScan]
----
Return to '''[http://compbio.chemistry.uq.edu.au/mediawiki/index.php/N-acetylneuraminic_acid_phosphatase Home Page]'''

Latest revision as of 01:26, 12 June 2007

Chain Sequence

MGSDKIHHHHHHMGLSRVRAVFFDLDNTLIDTAGASRRGMLEVIKLLQSKYHYKEEAEIICDKVQVKLSKECFHPYSTCI TDVRTSHWEEAIQETKGGADNRKLAEECYFLWKSTRLQHMILADDVKAMLTELRKEVRLLLLTNGDRQTQREKIEACACQ SYFDAIVIGGEQKEEKPAPSIFYHCCDLLGVQPGDCVMVGDTLETDIQGGLNAGLKATVWINKSGRVPLTSSPMPHYMVS SVLELPALLQSIDCKVSMSV

structure 18
interpro










































DALI Search Results

SUMMARY: PDB/chain identifiers and structural alignment statistics
NR. STRID1 STRID2  Z   RMSD LALI LSEQ2 %IDE REVERS PERMUT NFRAG TOPO PROTEIN
 1: 3033-A 2gfh-A 41.1  0.0  246   246  100      0      0     1 S    HYDROLASE        haloacid dehalogenase-like hydrolase domain
 2: 3033-A 1fez-A 18.1  3.5  178   256   22      0      0    13 S    HYDROLASE        phosphonoacetaldehyde hydrolase         (bacillus c 
 3: 3033-A 2hsz-A 17.9  3.3  168   222   23      0      0    13 S    STRUCTURAL GENOMICS, UNKNOWN FUNCTION    novel predicted
 4: 3033-A 1qq5-A 17.3  3.1  198   245   19      0      0    12 S    HYDROLASE        l-2-haloacid dehalogenase       (xanthobacter aut 
 5: 3033-A 1o03-A 17.0  5.0  188   221   20      0      0    11 S    ISOMERASE        beta-phosphoglucomutase         (lactococcus lactis
 6: 3033-A 2b0c-A 16.4  2.6  184   199   20      0      0    13 S    STRUCTURAL GENOMICS, UNKNOWN FUNCTION    putative phospha 
 7: 3033-A 2fdr-A 15.8  4.4  190   214   19      0      0    15 S    STRUCTURAL GENOMICS, UNKNOWN FUNCTION    conserved hypoth
 8: 3033-A 2p11-A 15.7  2.9  194   211   16      0      0    20 S    STRUCTURAL GENOMICS, UNKNOWN FUNCTION    hypothetical pro 
 9: 3033-A 1te2-A 15.7  3.6  170   211   19      0      0    15 S    HYDROLASE        putative phosphatase    (escherichia coli o157
10: 3033-A 1yns-A 15.3  4.0  169   254   11      0      0    13 S    HYDROLASE        e-1 enzyme (enolase-phosphatase e1)     (homo s 
11: 3033-A 1qyi-A 15.0  3.5  198   375   19      0      0    17 S    STRUCTURAL GENOMICS, UNKNOWN FUNCTION    hypothetical pro
12: 3033-A 2i6x-A 14.9  3.1  176   199   19      0      0    18 S    HYDROLASE        hydrolase, haloacid dehalogenase-like family 
13: 3033-A 1u7p-A 14.3  2.9  144   164   18      0      0    14 S    HYDROLASE        magnesium-dependent phosphatase-1 (mdp-1)       (
14: 3033-A 1ymq-A 14.1  2.3  130   260   16      0      0    14 S    TRANSFERASE      sugar-phosphate phosphatase bt4131      (bacte 
15: 3033-A 1j8d-A 13.1  2.5  141   180   11      0      0    12 S     HYDROLASE       deoxy-d-mannose-octulosonate 8-phosphate ph
16: 3033-A 2ho4-A 12.9  2.4  131   246   19      0      0    14 S    HYDROLASE        haloacid dehalogenase-like hydrolase domain 
17: 3033-A 1pw5-A 12.7  2.3  136   246   21      0      0    12 S    STRUCTURAL GENOMICS, UNKNOWN FUNCTION    nagd protein, pu
18: 3033-A 1nf2-A 12.7  2.6  127   267   13      0      0    11 S    STRUCTURAL GENOMICS/UNKNOWN FUNCTION     phosphatase     (the 
19: 3033-A 1rlm-A 12.4  2.8  131   269   13      0      0    14 S    HYDROLASE        phosphatase Mutant      (escherichia coli) bacte
20: 3033-A 1f5s-A 12.1  3.5  159   210   14      0      0    15 S     HYDROLASE       phosphoserine phosphatase (psp)         (methanoco 
21: 3033-A 1cr6-B 12.0  3.8  177   541   18      0      0    18 S    HYDROLASE        epoxide hydrolase       (mus musculus) mouse expr
22: 3033-A 1rku-A 11.9  3.6  172   206   11      0      0    18 S    TRANSFERASE      homoserine kinase       (pseudomonas aeruginosa 
23: 3033-A 2b30-A 11.8  2.7  134   284   16      0      0    12 S    STRUCTURAL GENOMICS, UNKNOWN FUNCTION    pvivax hypotheti
24: 3033-A 1kyt-A 10.5  2.5  122   216   13      0      0    15 S    STRUCTURAL GENOMICS, UNKNOWN FUNCTION    hypothetical  pro 
25: 3033-A 2o2x-A 10.3  3.6  139   204   17      0      0    14 S    STRUCTURAL GENOMICS, UNKNOWN FUNCTION    hypothetical pro
26: 3033-A 1u02-A 10.1  2.7  128   222   16      0      0    12 S    STRUCTURAL GENOMICS      trehalose-6-phosphate phosphatase 
27: 3033-A 2fea-A 10.0  3.5  167   219    7      0      0    21 S    HYDROLASE        2-hydroxy-3-keto-5-methylthiopentenyl-1- pho
28: 3033-A 2hx1-A  9.6  3.2  130   275   24      0      0    19 S    HYDROLASE        predicted sugar phosphatases of the had supe 
29: 3033-A 1mh9-A  9.2  3.2  146   194   15      0      0    15 S    HYDROLASE        deoxyribonucleotidase (mitochondrial  5'(3')-

Surface properties

Surface properties.JPG

From PDB

Chemical component identifier would be

PO4 PHOSPHATE ION

NA SODIUM ION

EDO 1,2-ETHANEDIOL

CL CHLORIDE ION

Closely related to 2HO4,PO4 PHOSPHATE ION found.

Cloesly related to 2HX1,CL Chloride Ion, EDO 1 2 Ethanediol found.

2GFH http://www.rcsb.org/pdb/explore/biologyAndChemistry.do?structureId=2GFH

2HX1 http://www.rcsb.org/pdb/explore/biologyAndChemistry.do?structureId=2HX1

1FEZ http://www.rcsb.org/pdb/explore/biologyAndChemistry.do?structureId=1FEZ

2HO4 http://www.rcsb.org/pdb/explore/biologyAndChemistry.do?structureId=2HO4

Pubmed

The identity of Asp12 as the active-site nucleophile was further evidenced by the observed removal of catalytic activity resulting from Asp12Ala substitution http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=10956028


Pfarm classification

PFAM Accession:PF00702

PFAM ID:hydrolase

http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00702

CE

2GFH USR1:A(size=260) vs 1FEZ USR2:A(size=256) Structure Alignment

2GFH USR1:A - MOL_ID: 1; MOLECULE: HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN CONTAINING 4; CHAIN: A; ENGINEERED: YES

1FEZ USR2:A - MOL_ID: 1; MOLECULE: PHOSPHONOACETALDEHYDE HYDROLASE; CHAIN: A, B, C, D; ENGINEERED: YES 


 USR1:A   17/6     RVRAVFFDLDNTLID-TAGASRRGMLEVIKLLQSKYHYKEEAEIICDKVQVKLSKECFHP
 USR2:A    1/6     KIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRG--------VAITAEEARKPMGLL----
 USR1:A   76/#12   YSTCITDVRTSHWEEA--IQETKG---GADN--RKLAEECYFLWKST--RLQHMILADDV
 USR2:A   49/54    -----KIDHVRALTEMPRIASEWNRVFRQLPTEADIQEMYEEFEEILFAILPRYASPINA
 USR1:A  127/116   KAMLTELRK--EVRLLLLTNGDRQTQREKIEACACQ-----SYFDAIVIGGEQKEEKPAP
 USR2:A  104/109   VKEVIASLRERGIKIGSTTG----YTREMMDIVAKEAALQGYKPDFLVTPDDVPAGRPYP
 USR1:A  180/169   SIFYHCCDLLGVQP-GDCVMVGDTLETDIQGGLNAGLKATVWINK---------------
 USR2:A  160/165   WMCYKNAMELGVYPMNHMIKVGDTVSDMKEGRNAGM--WTVGVILGSSELGLTEEEVENM
 USR1:A  224/213   --------SGR-VPLTSSPMPHYMVSSVLELPALLQSI
 USR2:A  218/223   DSVELREKIEVVRNRFVENGAHFTIETMQELESVMEHI

2gfh USR1:A - MOL_ID: 1; MOLECULE: HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN CONTAINING 4; CHAIN: A; ENGINEERED: YES

2hx1 USR2:A - MOL_ID: 1; MOLECULE: PREDICTED SUGAR PHOSPHATASES OF THE HAD SUPERFAMILY; CHAIN: A, B, C, D; ENGINEERED: YES 


 USR1:A   65/54    QVKLSKECFHPYST------------------------------CITDVRTSHWEEAIQE
 USR2:A   24/24    VLKTYNGL------LPGIENTFDYLKAQGQDYYIVTNDASRSPEQLADSYHKL-------
 USR1:A   95/84    TKGGADNRKLAEECYFLWKSTRLQHM---ILADDVKAMLTELRKEVRLLLLTNGDRQTQR
 USR2:A   71/71    ----------GLFSI-TADKIISSGXITKEYIDLKVDGG-------IVAYLG------TA
 USR1:A  152/141   EKIEACACQSYFDAIV-----------------IGGEQKEEKPAPSIFYHCCDLLGVQPG
 USR2:A  107/107   NSANY-LVSDGIKXLPVSAIDDSNIGEVNALVLLDDEGF------NWFHDLNKTVNLLRK
 USR1:A  195/184   DC-VMVGDTL---------------ETDIQGGLNAGLKATVWI
 USR2:A  160/160   RTIPAIVANTDNTYPLTKTDVAIAIGGVATXIES-ILGRRFIR

2gfh USR1:A - MOL_ID: 1; MOLECULE: HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN CONTAINING 4; CHAIN: A; ENGINEERED: YES

2ho4 USR2:A - MOL_ID: 1; MOLECULE: HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN CONTAINING 2; CHAIN: A, B; ENGINEERED: YES 


 USR1:A  122/111   LADDVKAMLTELRKEV--RLLLLTNGDRQTQREKIEACACQSYFD---------AIVIGG
 USR2:A   71/72    EIFTSLTAARNLIEQKQVRPXLLLD-----------DRALPEFTGVQTQDPNAVVIGLAP
 USR1:A  171/160   EQKEEKPAPSIFYHCCDLLGVQPGDCVMVGD-------------TLETDIQGGLNAGLKA
 USR2:A  120/121   EH----FHYQLLNQAFRLLLDG--APLIAIHKARYYKRKDGLALGPGPFVTALEYATDTK
 USR1:A  218/207   TVWINKSGRVPLTSSPMPHYMVSSVLELP
 USR2:A  174/175   AXV--------------------VGKPEK

2gfh and 2hx1.JPG

2gfh vs 2hx1 Rmsd = 5.6Å Z-Score = 3.1 Sequence identity = 6.2% Aligned/gap positions = 112/111


2gfh and 1fez.JPG

2gfh vs 1fez Rmsd = 4.4Å Z-Score = 5.5 Sequence identity = 17.4% Aligned/gap positions = 213/65


2gfh and 2ho4.JPG

2gfh vs 2ho4 Rmsd = 5.0Å Z-Score = 3.3 Sequence identity = 11.4% Aligned/gap positions = 88/61

ProFunc

http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/profunc/GetResults.pl?source=profunc&user_id=bb32&code=143144

Conserved.JPG

Diagram showing the conserved region ASN15 , Thr16, Leu17 with EDO4 molecule in grey and PO4 in yellow.

Po4 ligand.JPG

IMPORTANT!!! This is involved in the function. Most likely a phosphatase.

Edo4 ligand.JPG

Most likely an antifreezer.

Clefts.JPG

Possible binding sites. Results shows 2 ligands PO4 and EDO4

Pfam 21.0 (Janelia Farm)Alignments of top-scoring domains

Table of functions
Model

Hydrolase

Seq-from:18

Seq-to:224

HMM-from:1

HMM-to:183

Score:96.2

E-value:1e-25

Alignment:glocal

Description:haloacid dehalogenase-like hydrolase 

  Hydrolase: domain 1 of 1, from 18 to 224: score 96.2, E = 1e-25
                  *->ikavvFDkDGTLtdgkeppiaeaiveaaaelgl.........lplee
                     ++av+FD+D+TL+d+ + + ++ + e+ ++l  + + +++ ++  + 
      query    18    VRAVFFDLDNTLIDT-AGASRRGMLEVIKLLQSkyhykeeaeIICDK 63   

                  vekllgrgl.g.erilleggltaell...................d.evl
                  v   l +++ ++    ++   t ++ +   +++++ ++++  ++    ++
      query    64 VQVKLSKECfHpYSTCITDVRTSHWEeaiqetkggadnrklaeecYfLWK 113  

                  glial.dklypgarealkaLkrrGikvailTggdr.naeallealgla.l
                   ++ ++  l +++++ l +L++  +++ +lT+gdr++++++ ea+++ ++
      query   114 STRLQhMILADDVKAMLTELRKE-VRLLLLTNGDRqTQREKIEACACQsY 162  

                  fdviidsdevggvgpivvgKPkpeifllalerlgvkpeevgpevlmVGDg
                  fd+i++++e +        KP+p if + ++ lgv+p ++    +mVGD+
      query   163 FDAIVIGGEQK------EEKPAPSIFYHCCDLLGVQPGDC----VMVGDT 202  

                  vnDapalaa.AGv.gvamgngg<-*
                  + +++ +  +AG+++++++n +   
      query   203 LETDIQGGLnAGLkATVWINKS    224


External Link

1. EBI Mcromolecular Structure Database

2. InterProScan



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