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4OQH

Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying R164S mutation in complex with boron-based inhibitor EC25

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 Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 301
ChainResidue
AASP100
AASN135
ALEU136
ATHR139
AHOH436

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 302
ChainResidue
AHOH431
AHOH431
AGLU36
AGLU36
AHOH430
AHOH430

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 2UL A 303
ChainResidue
AMET68
ASER69
AGLU103
ASER129
AASN131
AGLU165
ALEU168
AASN169
ALYS233
ASER234
AGLY235
AALA236
AARG242
AHOH611
AHOH642
AHOH705

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

225946

PDB entries from 2024-10-09

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