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4OPQ

Room temperature crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying R164S/G238S mutations

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
AHOH402
AHOH402

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PG4 A 302
ChainResidue
AGLN98
AGLU109
AGLU146
ASER81
AARG82
AGLN87

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 303
ChainResidue
ATHR139
ATRP228
AILE284
AHOH512

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 304
ChainResidue
ASER202
AHOH466
AHOH504

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
ASER69
ASER129
AVAL215
ALYS233
ASER234
AGLY235
AALA236
AARG242
AHOH459

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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