Structure of PDB 5a5z Chain A

Receptor sequence
>5a5zA (length=236) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
QQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRV
LVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAG
IATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGPLKVFYPG
PGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAF
GAAFPKASMIVMSHSAPDSRAAITHTARMADKLRLE
3D structure
PDB5a5z Approved Drugs Containing Thiols as Inhibitors of Metallo-beta-lactamases: Strategy To Combat Multidrug-Resistant Bacteria.
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H120 H122 D124 H189 C208 K211 N220 H250
Catalytic site (residue number reindexed from 1) H84 H86 D88 H153 C172 K175 N184 H214
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 ZN A H120 H122 H189 H84 H86 H153
BS02 ZN A D124 H250 D88 H214
BS03 WJZ A D124 H189 N220 H250 D88 H153 N184 H214 PDBbind-CN: -logKd/Ki=4.08,IC50=84uM
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5a5z, PDBe:5a5z, PDBj:5a5z
PDBsum5a5z
PubMed25815530
UniProtC7C422|BLAN1_KLEPN Metallo-beta-lactamase type 2 (Gene Name=blaNDM-1)

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