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5OX2

Crystal structure of thymoligase, a substrate-tailored peptiligase variant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SO4 A 301
ChainResidue
APRO172
ASER173
AARG247

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 302
ChainResidue
ALYS237
AALA274
AGLN275

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 303
ChainResidue
ASER260
ALYS256
AGLY258
AASP259

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 A 304
ChainResidue
ATHR158
AGLY160

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDSGIdssH
ChainResidueDetails
AVAL28-HIS39

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVLA
ChainResidueDetails
AHIS64-ALA74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818
ChainResidueDetails
AASP32
AHIS64
AALA230

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
ALYS2
AASP41
AVAL75
APRO86
AALA88
ALEU90
AGLY178
AVAL180
ASER183

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 723
ChainResidueDetails
AASP32electrostatic interaction, electrostatic stabiliser
AHIS64proton acceptor, proton donor
ATHR164electrostatic interaction, electrostatic stabiliser
AALA230nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-11-06

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