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3BV9

Structure of Thrombin Bound to the Inhibitor FM19

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
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NH2 C 406
ChainResidue
BTRP148
CDAL404
C4PH405

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 302
ChainResidue
BHIS91

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD B 303
ChainResidue
BMET84
BLYS110
BHOH519

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 307
ChainResidue
BHOH331
BHOH336
BHOH362
BHOH376
BARG221
BLYS224

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 305
ChainResidue
BPRO92
BTRP237

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL B 306
ChainResidue
BASN60

site_idAC7
Number of Residues23
DetailsBINDING SITE FOR CHAIN C OF FM19 INHIBITOR
ChainResidue
BHIS57
BTYR60
BTRP60
BASN98
BTHR147
BTRP148
BILE174
BASP189
BALA190
BCYS191
BGLU192
BSER195
BVAL213
BTRP215
BGLY216
BGLY219
BGLY226
BHOH322
BHOH347
BHOH407
CHOH59
CHOH77
CHOH83

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 Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BHIS57
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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BHIS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER195
BGLY193

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER195
BGLY196

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57
BGLY196

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BGLY193
BHIS57

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PDB entries from 2024-11-13

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