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1F13

RECOMBINANT HUMAN CELLULAR COAGULATION FACTOR XIII

Functional Information from GO Data
ChainGOidnamespacecontents
A0003810molecular_functionprotein-glutamine gamma-glutamyltransferase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0007596biological_processblood coagulation
A0007599biological_processhemostasis
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0018149biological_processpeptide cross-linking
A0031012cellular_componentextracellular matrix
A0031093cellular_componentplatelet alpha granule lumen
A0046872molecular_functionmetal ion binding
A0072378biological_processblood coagulation, fibrin clot formation
A0072562cellular_componentblood microparticle
A1990234cellular_componenttransferase complex
B0003810molecular_functionprotein-glutamine gamma-glutamyltransferase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0007596biological_processblood coagulation
B0007599biological_processhemostasis
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0018149biological_processpeptide cross-linking
B0031012cellular_componentextracellular matrix
B0031093cellular_componentplatelet alpha granule lumen
B0046872molecular_functionmetal ion binding
B0072378biological_processblood coagulation, fibrin clot formation
B0072562cellular_componentblood microparticle
B1990234cellular_componenttransferase complex
Functional Information from PDB Data
site_idCT1
Number of Residues3
DetailsCATALYTIC TRIAD OF SUBUNIT 1 COMPRISING THE ACTIVE SITE.
ChainResidue
ACYS314
AHIS373
AASP396

site_idCT2
Number of Residues3
DetailsCATALYTIC TRIAD OF SUBUNIT 2 COMPRISING THE ACTIVE SITE.
ChainResidue
BCYS314
BHIS373
BASP396

Functional Information from PROSITE/UniProt
site_idPS00547
Number of Residues18
DetailsTRANSGLUTAMINASES Transglutaminases active site. GQCWVfAGVfnTfLRCLG
ChainResidueDetails
AGLY312-GLY329

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"evidences":[{"source":"PubMed","id":"7913750","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9988734","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1g0d
ChainResidueDetails
ACYS314
AASP396
AHIS373
ATYR560

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1g0d
ChainResidueDetails
BCYS314
BASP396
BHIS373
BTYR560

site_idMCSA1
Number of Residues5
DetailsM-CSA 149
ChainResidueDetails
ATRP279electrostatic stabiliser, hydrogen bond donor
ACYS314electrostatic stabiliser
AHIS373electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASP396electrostatic stabiliser, hydrogen bond acceptor
ATYR560electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 149
ChainResidueDetails
BTRP279electrostatic stabiliser, hydrogen bond donor
BCYS314electrostatic stabiliser
BHIS373electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASP396electrostatic stabiliser, hydrogen bond acceptor
BTYR560electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-07-30

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