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1GGT

THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD 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
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
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 PDB Data
site_idCAT
Number of Residues3
DetailsCATALYTIC TRIAD RESIDUES IN CHAIN A
ChainResidue
ACYS314
AHIS373
AASP396

site_idCBT
Number of Residues3
DetailsCATALYTIC TRIAD RESIDUES IN CHAIN B
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
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:7913750
ChainResidueDetails
ATRP315
ACYS374
ASER397
BTRP315
BCYS374
BSER397

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:9988734
ChainResidueDetails
ASER437
ALEU439
AGLY486
AARG491
BSER437
BLEU439
BGLY486
BARG491

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by thrombin; to produce active factor XIII-A
ChainResidueDetails
AGLY38
BGLY38

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000305|PubMed:2877456
ChainResidueDetails
AGLU2
BGLU2

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AGLU614
BGLU614

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
AASP280electrostatic stabiliser, hydrogen bond donor
ATRP315electrostatic stabiliser
ACYS374electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ASER397electrostatic stabiliser, hydrogen bond acceptor
ATHR561electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 149
ChainResidueDetails
BASP280electrostatic stabiliser, hydrogen bond donor
BTRP315electrostatic stabiliser
BCYS374electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BSER397electrostatic stabiliser, hydrogen bond acceptor
BTHR561electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-10-30

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