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4RKJ

Crystal structure of thrombin mutant S195T (free form)

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 K A 301
ChainResidue
ATYR14
ATYR14
BTYR134
BTYR134
BHOH597
BHOH597

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
BGLU127
BSER129
BPHE204
BHOH482
BHOH505
AGLU14
AASP14
BARG97

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
BASP189
BALA190
BTRP215
BGLY216
BGLY219
BHOH473

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BILE162
BVAL163
BARG165
BCYS168
BPHE181
BCYS182
BHOH585

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BHIS57
BASP102
BTHR195

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

224572

PDB entries from 2024-09-04

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