Structure of PDB 5ne3 Chain A

Receptor sequence
>5ne3A (length=269) Species: 522373 (Stenotrophomonas maltophilia K279a) [Search protein sequence]
APTDAAITAASDFAALEKACAGRLGVTLLDTASGRRIGHRQDERFPMCST
FKSMLAATVLSQAERMPALLDRRVPVGEADLLSHAPVTRRHAGKDMTVRD
LCRATIITSDNTAANLLFGVVGGPPAVTAFLRASGDTVSRSDRLEPELNS
FAKGDPRDTTTPAAMAATLQRVVLGEVLQPASRQQLADWLIDNETGDACL
RAGLGKRWRVGDKTGSNGEDARNDIAVLWPVAGGAPWVLTAYLQAGAISY
EQRASVLAQVGRIADRLIG
3D structure
PDB5ne3 Structural/mechanistic insights into the efficacy of nonclassical beta-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates.
ChainA
Resolution1.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S69 K72 S129 E165 K233 S236
Catalytic site (residue number reindexed from 1) S49 K52 S109 E145 K213 S216
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 S69 H104 S129 N131 N169 T215 T234 G235 S236 S49 H84 S109 N111 N149 T195 T214 G215 S216 PDBbind-CN: -logKd/Ki=7.84,IC50=14.36nM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic

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Molecular Function
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Biological Process
External links
PDB RCSB:5ne3, PDBe:5ne3, PDBj:5ne3
PDBsum5ne3
PubMed28876489
UniProtB2FRP5

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