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1EX0

HUMAN FACTOR XIII, MUTANT W279F ZYMOGEN

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_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1320
ChainResidue
AASN436
AASP438
AALA457
AHOH1518
AHOH1646

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 1321
ChainResidue
BHOH1417
BHOH1536
BHOH1692
BASN436
BSER437
BASP438
BALA457

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 1330
ChainResidue
AASP456
ATHR458
AHIS459
ALYS462
ALYS621
AHOH1473
AHOH1550

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 B 1331
ChainResidue
BASP456
BTHR458
BHIS459
BLYS462
BLYS621
BHOH1372
BHOH1595
BHOH1664
BHOH1867

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 1332
ChainResidue
BASN517
BSER543
BHIS544

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGO A 1340
ChainResidue
AARG260
AASP404
ATYR407
AARG408
AHOH1376
AHOH1386
BASP404
BARG408

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGO A 1341
ChainResidue
AGLN85
AMET136
AGLU138
ASER141
AVAL142
AARG143

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGO A 1342
ChainResidue
ATYR500
BPHE424

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGO B 1343
ChainResidue
BGLU525
BLYS534
BHOH1760
BHOH1964

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGO B 1344
ChainResidue
BLYS565
BGLY596
BGLN597
BHOH2068

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGO B 1345
ChainResidue
BGLU571
BGLU585
BALA586
BVAL587
BHOH1438
BHOH1732

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
ASER397
ATRP315
ACYS374
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_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
BTRP315electrostatic stabiliser
BCYS374electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BSER397electrostatic stabiliser, hydrogen bond acceptor
BTHR561electrostatic stabiliser, hydrogen bond donor
BASP280electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-05-29

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