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1K4F

CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10 AT 1.6 A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
AARG160
AHOH860
AHOH872
AHOH900
AHOH904
BHOH850

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 702
ChainResidue
ATHR206
AGLY207
APHE208
AARG250
AHOH847
AHOH905
AHOH1000
ASER67
ASER115
ALYS205

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 703
ChainResidue
BSER67
BSER115
BLYS205
BTHR206
BGLY207
BPHE208
BARG250

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 704
ChainResidue
BARG160
BHOH905
BHOH924

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnAI
ChainResidueDetails
APRO65-ILE75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate
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:11188693
ChainResidueDetails
AKCX70
BKCX70

218853

PDB entries from 2024-04-24

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