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4BDV

CRYSTAL STRUCTURE OF A TRUNCATED B-DOMAIN HUMAN FACTOR VIII

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
B0005507molecular_functioncopper ion binding
B0016491molecular_functionoxidoreductase activity
Functional Information from PROSITE/UniProt
site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GqFlLfChISshQhDGMeayV
ChainResidueDetails
AGLY304-VAL324
AGLY686-LEU706
BGLY1994-PHE2014

site_idPS01285
Number of Residues28
DetailsFA58C_1 Coagulation factors 5/8 type C domain (FA58C) signature 1. AWstkepfs........WIkVDllapmiIhgIkTQG
ChainResidueDetails
BALA2061-GLY2088
BALA2218-GLY2247

site_idPS01286
Number of Residues17
DetailsFA58C_2 Coagulation factors 5/8 type C domain (FA58C) signature 2. Pthysirst..LRmELmGC
ChainResidueDetails
BPRO2153-CYS2169
BPRO2310-CYS2326

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Cleavage (activation)
ChainResidueDetails
BARG1648
AARG740

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by thrombin
ChainResidueDetails
BARG1689

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Sulfotyrosine => ECO:0000269|PubMed:10368977, ECO:0000269|PubMed:1554716
ChainResidueDetails
BTYR1664
ATYR719
ATYR723

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Sulfotyrosine => ECO:0000269|PubMed:10368977, ECO:0000269|PubMed:1554716, ECO:0000269|PubMed:1898735
ChainResidueDetails
BTYR1680
AASN239

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN1810
BASN2118

227344

PDB entries from 2024-11-13

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