Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8CMT

Structure of the plasma coagulation Factor XIII A2B2 heterotetrameric complex.

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
A0031093cellular_componentplatelet alpha granule lumen
A0046872molecular_functionmetal ion binding
A0062023cellular_componentcollagen-containing extracellular matrix
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
B0031093cellular_componentplatelet alpha granule lumen
B0046872molecular_functionmetal ion binding
B0062023cellular_componentcollagen-containing extracellular matrix
B0072378biological_processblood coagulation, fibrin clot formation
B0072562cellular_componentblood microparticle
B1990234cellular_componenttransferase complex
Functional Information from PROSITE/UniProt
site_idPS00547
Number of Residues18
DetailsTRANSGLUTAMINASES Transglutaminases active site. GQCWVfAGVfnTfLRCLG
ChainResidueDetails
AGLY313-GLY330

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
CASN162
DASN162
AASP397
BCYS315
BHIS374
BASP397

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
CASN545
DASN545
AGLU486
AGLU491
BASN437
BASP439
BGLU486
BGLU491

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by thrombin; to produce active factor XIII-A
ChainResidueDetails
AARG38
BARG38

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000305|PubMed:2877456
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN614
BASN614

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 149
ChainResidueDetails
ATRP280electrostatic stabiliser, hydrogen bond donor
ACYS315electrostatic stabiliser
AHIS374electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASP397electrostatic stabiliser, hydrogen bond acceptor
ATYR561electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 149
ChainResidueDetails
BTRP280electrostatic stabiliser, hydrogen bond donor
BCYS315electrostatic stabiliser
BHIS374electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASP397electrostatic stabiliser, hydrogen bond acceptor
BTYR561electrostatic stabiliser, hydrogen bond donor

235183

PDB entries from 2025-04-23

PDB statisticsPDBj update infoContact PDBjnumon