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4OPR

Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S mutation

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AGLU36
AGLU36
AHOH401
AHOH401
AHOH403
AHOH403

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PG4 A 302
ChainResidue
AGLN87
AGLN98
ALEU101
AGLU109
AGLU146
APHE150
AHOH569
AHOH671
AALA78
ASER81
AARG82

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
ASER69
ASER129
AVAL215
ALYS233
ASER234
AGLY235
AALA236
AARG242
AHOH431

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL
ChainResidueDetails
APHE65-LEU80

226707

PDB entries from 2024-10-30

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