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4KTY

Fibrin-stabilizing factor with a bound ligand

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 Residues8
DetailsBINDING SITE FOR RESIDUE DAS C 2
ChainResidue
ATYR214
AARG223
AGLN313
AASN371
ATYR372
CACY1
C1TX3
CABA4

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE DAS D 2
ChainResidue
BARG223
BGLN313
BASN371
BTYR372
DACY1
D1TX3
DABA4
DHOH107
BTYR214

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 801
ChainResidue
AALA264
AASN267
ALYS269
AASP271
AHOH906

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 802
ChainResidue
AASP343
AASP345
AASN347
AGLN349
AASP351
AASP367

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 803
ChainResidue
AASN436
AALA457
AGLU485
AGLU490
AHOH908
AHOH909

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 804
ChainResidue
ATYR194
ALEU195
AASP196
ATRP379
APHE559
ATHR561
AHOH929
AHOH1269

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 805
ChainResidue
APHE53
AASP58
ATHR59
ATYR83
AHOH974
AHOH1151

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 806
ChainResidue
AVAL287
AGLU301
AVAL309
AARG310
AHOH1174

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 807
ChainResidue
AASN20
AGLU23
ALYS156
AARG158
AARG174
AASP179
AHOH979
AHOH1100
AHOH1326

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 808
ChainResidue
AARG715
AHIS716
AHOH1048
AHOH1303
BTRP164
BTHR165
BGLY168
BVAL169

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 809
ChainResidue
AASN541
AASN542
ALEU580
ASER581
BVAL39
BHOH1343

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 801
ChainResidue
BALA264
BASN267
BLYS269
BASP271
BHOH901

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 802
ChainResidue
BASP343
BASP345
BASN347
BGLN349
BASP351
BASP367

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 803
ChainResidue
BASN436
BALA457
BGLU485
BGLU490
BHOH973
BHOH1307

site_idBC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 804
ChainResidue
BHOH914
BHOH1104
BHOH1212
BTYR194
BLEU195
BASP196
BTRP379
BPHE559
BTHR561

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 805
ChainResidue
BPHE53
BASP58
BTHR59
BTYR83
BARG143
BHOH985
BHOH1178

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 806
ChainResidue
AHOH1285
BARG100
BTRP164
BHOH933
BHOH1306

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 807
ChainResidue
BLYS269
BASP270
BARG681
BHOH1131
BHOH1293
BHOH1304

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
ACYS314
AHIS373
AASP396
BCYS314
BHIS373
BASP396

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:9988734
ChainResidueDetails
AASN436
AASP438
AGLU485
AGLU490
BASN436
BASP438
BGLU485
BGLU490

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by thrombin; to produce active factor XIII-A
ChainResidueDetails
AARG37
BARG37

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000305|PubMed:2877456
ChainResidueDetails
ASER1
BSER1

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN613
BASN613

Catalytic Information from CSA
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 2024-08-21

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