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1NL0

Crystal structure of human factor IX Gla domain in complex of an inhibitory antibody, 10C12

Functional Information from GO Data
ChainGOidnamespacecontents
G0005509molecular_functioncalcium ion binding
G0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA G 901
ChainResidue
GCGU26
GCGU30

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA G 902
ChainResidue
GCGU8
GCGU27
GCGU30
GHOH921

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA G 903
ChainResidue
GCGU30
GHOH917
GCGU8
GCGU17
GCGU27

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA G 904
ChainResidue
GTYR1
GASN2
GCGU7
GCGU8
GCGU17
GCGU27

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA G 905
ChainResidue
GTYR1
GCGU7
GCGU17
GCGU21
GHOH912

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA G 907
ChainResidue
GCGU15
GCGU20

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 L 211
ChainResidue
LSER80
LGLN109
LTYR141
LLYS167
LHOH212

Functional Information from PROSITE/UniProt
site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EcmEEkCsfeearEvfentertte.FW
ChainResidueDetails
GCGU17-TRP42

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
ChainResidueDetails
HTYR194-HIS200
LTYR192-HIS198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14722079, ECO:0007744|PDB:1NL0
ChainResidueDetails
GTYR1
GASN2

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: via 4-carboxyglutamate => ECO:0000305|PubMed:14722079, ECO:0007744|PDB:1NL0
ChainResidueDetails
GCGU7
GCGU8
GCGU17
GCGU21
GCGU27

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: via 4-carboxyglutamate => ECO:0000250|UniProtKB:P00741
ChainResidueDetails
GCGU15
GCGU20
GCGU26
GCGU30
GCGU36
GCGU40

site_idSWS_FT_FI4
Number of Residues12
DetailsMOD_RES: 4-carboxyglutamate => ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463
ChainResidueDetails
GCGU7
GCGU33
GCGU36
GCGU40
GCGU8
GCGU15
GCGU17
GCGU20
GCGU21
GCGU26
GCGU27
GCGU30

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:25456591
ChainResidueDetails
GTHR39

225946

PDB entries from 2024-10-09

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