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1J35

Crystal Structure of Ca(II)-bound Gla Domain of Factor IX Complexed with Binding Protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0035821biological_processmodulation of process of another organism
A0046872molecular_functionmetal ion binding
A0090729molecular_functiontoxin activity
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
B0035821biological_processmodulation of process of another organism
B0046872molecular_functionmetal ion binding
B0090729molecular_functiontoxin activity
C0005509molecular_functioncalcium ion binding
C0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 501
ChainResidue
AGLU98
BHOH617
CCGU426
CCGU430

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 502
ChainResidue
BHOH643
CCGU408
CCGU427
CCGU430
CHOH655

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA C 503
ChainResidue
CCGU408
CCGU417
CCGU427
CCGU430
CHOH625
CHOH636
CHOH661

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 504
ChainResidue
CTYR401
CASN402
CCGU407
CCGU408
CCGU417
CCGU427

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 505
ChainResidue
CTYR401
CCGU407
CCGU417
CCGU421
CHOH692
CHOH705

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 506
ChainResidue
CCGU421
CHOH675
CHOH708
CHOH740
CHOH810

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA C 507
ChainResidue
CCGU415
CCGU420
CHOH776

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 508
ChainResidue
CCGU436
CCGU440
CHOH654
CHOH725
CHOH840

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 511
ChainResidue
ASER41
AGLU43
AGLU47
AGLU128
AHOH603
AHOH823

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 512
ChainResidue
BSER241
BGLN243
BGLU247
BGLU320
BHOH822
BHOH829

Functional Information from PROSITE/UniProt
site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EckEEkCsfeearEvfentektte.FW
ChainResidueDetails
CCGU417-TRP442

site_idPS00615
Number of Residues26
DetailsC_TYPE_LECTIN_1 C-type lectin domain signature. CLgleketgfrk..WVNIYCgqqnp.FVC
ChainResidueDetails
ACYS102-CYS127
BCYS296-CYS319

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues250
DetailsDomain: {"description":"C-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10339409","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12695512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16165155","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1J34","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1J35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X2T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10339409","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12695512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16165155","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9187649","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IXX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1J34","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1J35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X2T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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