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6V64

Crystal structure of human thrombin bound to ppack with tryptophans replaced by 5-F-tryptophan

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 Residues6
Detailsbinding site for residue NA A 101
ChainResidue
ATYR14
ATYR14
AHOH203
AHOH203
BTYR134
BTYR134

site_idAC2
Number of Residues20
Detailsbinding site for residue 0G6 B 301
ChainResidue
BGLU97
BLEU99
BASP189
BALA190
BGLY193
BSER195
BSER214
BFTR215
BGLY216
BGLY219
BCYS220
BGLY226
BLYS236
BHOH405
BHOH425
BHOH435
BHOH448
BHIS57
BTYR60
BFTR60

site_idAC3
Number of Residues6
Detailsbinding site for residue NA B 302
ChainResidue
BARG221
BLYS224
BHOH406
BHOH427
BHOH434
BHOH462

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

226262

PDB entries from 2024-10-16

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