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4OP5

Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying R164S 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
AHOH408
AHOH408

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PG4 A 302
ChainResidue
AALA85
AGLN87
AGLN98
ALEU101
AGLU109
ALEU112
AGLU146
APHE150
AHOH547
AHOH591
AALA78
ASER81
AARG82

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MES A 303
ChainResidue
ASER69
ASER129
ALYS191
AVAL215
ALYS233
ASER234
AGLY235
AALA236
AARG242
AHOH422

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

221716

PDB entries from 2024-06-26

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