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9L6Q

Vitamin K-dependent gamma-carboxylase in complex with Coagulation factor IX and vitamin K

Functional Information from GO Data
ChainGOidnamespacecontents
A0005788cellular_componentendoplasmic reticulum lumen
A0005789cellular_componentendoplasmic reticulum membrane
A0007596biological_processblood coagulation
A0008289molecular_functionlipid binding
A0008488molecular_functiongamma-glutamyl carboxylase activity
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0017187biological_processpeptidyl-glutamic acid carboxylation
A0019842molecular_functionvitamin binding
A0036211biological_processprotein modification process
A0042373biological_processvitamin K metabolic process
A0046929biological_processnegative regulation of neurotransmitter secretion
A0051604biological_processprotein maturation
A1903011biological_processnegative regulation of bone development
A2000225biological_processnegative regulation of testosterone biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDdinsYeCwC
ChainResidueDetails
CCYS108-CYS119

site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EcmEEkCsfeearEvfentertte.FW
ChainResidueDetails
CGLU63-TRP88

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CwCpfGfeGKnC
ChainResidueDetails
CCYS117-CYS128

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
ChainResidueDetails
CVAL263-CYS268

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPHV
ChainResidueDetails
CASP405-VAL416

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CwCpfGFegkn....C
ChainResidueDetails
CCYS117-CYS128
CCYS155-CYS170

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCesnp..........Clnggs..CkDdinsYeC
ChainResidueDetails
CASP93-CYS117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues100
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues165
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17073445","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues17
DetailsPropeptide: {"featureId":"PRO_0000027755","evidences":[{"source":"PubMed","id":"2592373","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14722079","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NL0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
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_FI9
Number of Residues2
DetailsModified residue: {"description":"4-carboxyglutamate","evidences":[{"source":"UniProtKB","id":"P00741","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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