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1IXA

THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST EGF-LIKE MODULE OF HUMAN FACTOR IX: COMPARISON WITH EGF AND TGF-A

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDdinsYeCwC
ChainResidueDetails
ACYS62-CYS73

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CwCpfGfeGKnC
ChainResidueDetails
ACYS71-CYS82

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CwCpfGFegkn....C
ChainResidueDetails
ACYS71-CYS82

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCesnp..........Clnggs..CkDdinsYeC
ChainResidueDetails
AASP47-CYS71

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:7606779, ECO:0007744|PDB:1EDM
ChainResidueDetails
AASP47
AGLY48
AGLN50
AASP64
AASP65

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:6688526
ChainResidueDetails
AASP64

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|Ref.28
ChainResidueDetails
ASER68

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) serine => ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:2511201, ECO:0000269|PubMed:25456591
ChainResidueDetails
ASER53

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc...) serine => ECO:0000269|PubMed:1517205, ECO:0000269|PubMed:25456591
ChainResidueDetails
ASER61

226707

PDB entries from 2024-10-30

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