Structure of PDB 5ne1 Chain B

Receptor sequence
>5ne1B (length=270) Species: 40324 (Stenotrophomonas maltophilia) [Search protein sequence]
NAPTDAAITAASDFAALEKACAGRLGVTLLDTASGRRIGHRQDERFPMCS
TFKSMLAATVLSQAERMPALLDRRVPVGEADLLSHAPVTRRHAGKDMTVR
DLCRATIITSDNTAANLLFGVVGGPPAVTAFLRASGDTVSRSDRLEPELN
SFAKGDPRDTTTPAAMAATLQRVVLGEVLQPASRQQLADWLIDNETGDAC
LRAGLGKRWRVGDKTGSNGEDARNDIAVLWPVAGGAPWVLTAYLQAGAIS
YEQRASVLAQVGRIADRLIG
3D structure
PDB5ne1 Structural/mechanistic insights into the efficacy of nonclassical beta-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates.
ChainB
Resolution2.09 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 E166 K234 S237
Catalytic site (residue number reindexed from 1) S50 K53 S110 E146 K214 S217
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 OK3 B S70 H105 S130 N132 N170 T235 G236 S237 N238 G240 S50 H85 S110 N112 N150 T215 G216 S217 N218 G219 PDBbind-CN: -logKd/Ki=8.28,IC50=5.25nM
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:5ne1, PDBe:5ne1, PDBj:5ne1
PDBsum5ne1
PubMed28876489
UniProtQ9RBQ1

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