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1CFH

STRUCTURE OF THE METAL-FREE GAMMA-CARBOXYGLUTAMIC ACID-RICH MEMBRANE BINDING REGION OF FACTOR IX BY TWO-DIMENSIONAL NMR SPECTROSCOPY

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 48
ChainResidue
AGLU7
AGLU8

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 49
ChainResidue
ATYR1
AGLU8

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT A 50
ChainResidue
AGLU15

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 51
ChainResidue
AGLU17
ALYS22

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT A 52
ChainResidue
AGLU20

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 53
ChainResidue
ASER24
AGLU21

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT A 54
ChainResidue
AGLU26

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT A 55
ChainResidue
AGLU27

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 56
ChainResidue
AGLU30
AVAL31
APHE32

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 57
ChainResidue
APHE32
AGLU33

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT A 58
ChainResidue
AGLU36

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT A 59
ChainResidue
AGLU40

Functional Information from PROSITE/UniProt
site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EcmEEkCsfeearEvfentertte.FW
ChainResidueDetails
AGLU17-TRP42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues45
DetailsDomain: {"description":"Gla","evidences":[{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14722079","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NL0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"description":"via 4-carboxyglutamate","evidences":[{"source":"PubMed","id":"14722079","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NL0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"description":"via 4-carboxyglutamate","evidences":[{"source":"UniProtKB","id":"P00741","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7606779","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EDM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsModified residue: {"description":"4-carboxyglutamate","evidences":[{"source":"UniProtKB","id":"P00741","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"source":"PubMed","id":"25456591","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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