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1K38

CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-2

Functional Information from GO Data
ChainGOidnamespacecontents
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 401
ChainResidue
ASER115
ATHR206
AGLY207
ATRP208
AARG244
BASN96

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 402
ChainResidue
BTRP208
BARG244
AASN96
BSER115
BTHR206

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT B 403
ChainResidue
AHOH479
BPHE180
BARG181
BARG181
BHOH406
BHOH429
BHOH501

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPhTL
ChainResidueDetails
APRO65-LEU75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10103
ChainResidueDetails
ASER67
BSER67

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS205
BLYS205

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000269|PubMed:8240304
ChainResidueDetails
AKCX70
BKCX70

218853

PDB entries from 2024-04-24

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