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4RN6

Structure of prethrombin-2 mutant s195a bound to the active site inhibitor argatroban

Replaces:  4HFY
Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0007596biological_processblood coagulation
B0004252molecular_functionserine-type endopeptidase activity
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0007596biological_processblood coagulation
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 15U A 301
ChainResidue
AHIS57
ATYR60
ATRP60
ALEU144
ATRP148
ATRP215
AGLY216
AGLY219

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 15U B 301
ChainResidue
BTYR60
BTRP148
BVAL213
BSER214
BTRP215
BGLY216
BGLU217
BGLY219
BGLY226
BHIS57

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU53-CYS58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
AASP102
AALA195
BHIS57
BASP102
BALA195

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by factor Xa => ECO:0000269|PubMed:34265300
ChainResidueDetails
AARG15
BARG15

site_idSWS_FT_FI3
Number of Residues2
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
AASN60
BASN60

222415

PDB entries from 2024-07-10

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