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3KSR

CRYSTAL STRUCTURE OF A PUTATIVE SERINE HYDROLASE (XCC3885) FROM XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS AT 2.69 A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 290
ChainResidue
ATRP36
ATYR134
ALYS143
AASN147
AARG156
AILE188
AHOH300

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 291
ChainResidue
ALYS85
AARG121

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 292
ChainResidue
AASP186
AVAL187
AASP216
AHIS217

Functional Information from PROSITE/UniProt
site_idPS00708
Number of Residues31
DetailsPRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DikaAydqLaslpyvdahsiavvGlSyGGYL
ChainResidueDetails
AASP83-LEU113

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c4x
ChainResidueDetails
AASP186
AHIS217
ASER108

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PDB entries from 2025-07-30

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