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3B23

Crystal structure of thrombin-variegin complex: Insights of a novel mechanism of inhibition and design of tunable thrombin inhibitors

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0007596biological_processblood coagulation
B0004252molecular_functionserine-type endopeptidase activity
B0005509molecular_functioncalcium ion binding
B0006508biological_processproteolysis
B0007596biological_processblood coagulation
C0004867molecular_functionserine-type endopeptidase inhibitor activity
C0005576cellular_componentextracellular region
C0140678molecular_functionmolecular function inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR CHAIN C OF VARIEGIN
ChainResidue
BPHE34
BARG67
BARG73
BTHR74
BARG75
BTYR76
BARG77
BASN143
BTHR147
BTRP148
BVAL149
BGLN38
BGLN151
BARG173
BILE174
BGLU192
BGLU192
BSER195
BHOH266
CHOH33
CHOH34
CHOH49
BGLU39
CHOH50
CHOH278
BLEU40
BLEU41
BTYR60
BTRP60
BLYS60
BLEU65

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
BLEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
BASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: O-linked (Hex) threonine => ECO:0000269|PubMed:17684009
ChainResidueDetails
CTHR14
BASP102
BSER195

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923
ChainResidueDetails
BASN60

219140

PDB entries from 2024-05-01

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