Structure of PDB 6lc8 Chain A

Receptor sequence
>6lc8A (length=357) Species: 550 (Enterobacter cloacae) [Search protein sequence]
PMSEKQLADVVERTVTPLMKAQAIPGMAVAVIYQGQPHYFTFGKADVAAN
KPVTPQTLFELGSVSKTFTGVLGGDAIARKEISLADPVTKYWPELTGKQW
QGIRLLDLATYTAGGLPLQVPDNVTDNASLLRFYQSWQPKWAPGTTRLYA
NTSIGLFGSLAVKPSGMRFEQAMAERVFKPLKLNHTWINVPHAEESHYAW
GYREGKAVHVSPGMLDAEAYGVKSNVKDMASWVMANMAPETLPPSTLQQG
IALAQSRYWRVGAMYQGLGWEMLNWPVDVKTVVDGSDNKVALVPVAEVNP
PAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLANKSYPNPVRVETA
YRILETL
3D structure
PDB6lc8 Structural Basis of Reduced Susceptibility to Ceftazidime-Avibactam and Cefiderocol inEnterobacter cloacaeDue to AmpC R2 Loop Deletion.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y150 E272 K313 S316
Catalytic site (residue number reindexed from 1) S63 K66 Y149 E271 K312 S315
Enzyme Commision number 3.5.2.6: beta-lactamase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NXL A S64 Q120 Y150 N152 N289 T314 G315 S316 N344 S63 Q119 Y149 N151 N288 T313 G314 S315 N343
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6lc8, PDBe:6lc8, PDBj:6lc8
PDBsum6lc8
PubMed32284381
UniProtA0A0A0Q7Z8

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