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4XDE

Coagulation Factor XII protease domain crystal structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue IPA A 701
ChainResidue
ALEU371
ACYS394

site_idAC2
Number of Residues7
Detailsbinding site for residue IPA A 702
ChainResidue
ATRP373
ASER376
AASP397
ALEU524
APRO525
AHOH810
AHOH853

site_idAC3
Number of Residues6
Detailsbinding site for residue FLC A 703
ChainResidue
AVAL437
ASER438
ATYR439
ASER522
ATRP567
AHOH861

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU389-CYS394

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPLV
ChainResidueDetails
AASP538-VAL549

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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