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3LMS

Structure of human activated thrombin-activatable fibrinolysis inhibitor, TAFIa, in complex with tick-derived funnelin inhibitor, TCI.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
A0042730biological_processfibrinolysis
B0004857molecular_functionenzyme inhibitor activity
B0005575cellular_componentcellular_component
B0005576cellular_componentextracellular region
B0007596biological_processblood coagulation
B0008191molecular_functionmetalloendopeptidase inhibitor activity
B0010951biological_processnegative regulation of endopeptidase activity
B0030414molecular_functionpeptidase inhibitor activity
B0035821biological_processmodulation of process of another organism
B0044002biological_processacquisition of nutrients from host
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 309
ChainResidue
AHIS69
AGLU72
AHIS196
BLEU74

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GLY A 501
ChainResidue
BLEU74
AHIS69
AARG127
AASN144
AARG145
ATYR248

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 502
ChainResidue
BGLY39
BCYS40
BLYS41
BSER63

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
APHE132
AILE139
ACYS166
AGLY167
AHOH526
AHOH528
AHOH530

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 504
ChainResidue
ASER5
AGLY84
AHIS85
AGLN88

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 505
ChainResidue
ATRP73
AARG124
APHE279
ALEU280
ALEU281
BGLY7
BPHE8

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 506
ChainResidue
ATYR118

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 507
ChainResidue
AHIS137
ASER160
ACA509

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 508
ChainResidue
ACA509
BSER28

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 509
ChainResidue
ALYS122
ASER159
ACYS161
ACL507
BCL508

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K A 510
ChainResidue
AGLN95
AARG306

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K A 511
ChainResidue
AASN16
BGLY67

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379
ChainResidueDetails
AGLU270

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:18559974, ECO:0000269|PubMed:20088943
ChainResidueDetails
AHIS69
AGLU72
AHIS196

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00730
ChainResidueDetails
AARG127
AASN144
ASER197
ATYR248

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cleavage; by thrombin
ChainResidueDetails
AARG210

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:16445295
ChainResidueDetails
AASN129

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PDB entries from 2024-05-01

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