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3BYD

Crystal structure of beta-lactamase OXY-1-1 from Klebsiella oxytoca

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
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ASER73
ASER133
ALYS237
ATHR238
AGLY239
AALA240
AHOH524
AHOH570

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
ATRP232
APRO254
AGLU255
AASN256
AHIS257
AHOH557
ASER231

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AARG97
AGLU124
AGLY221
AHOH560

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AARG68
ALYS102
ALYS180
AGLU255
AHOH474
AHOH520

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 305
ChainResidue
AARG181
AHOH596

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FaMCSTgKvmaAAAVL
ChainResidueDetails
APHE69-LEU84

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10101
ChainResidueDetails
ASER73

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS237

218853

PDB entries from 2024-04-24

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