Structure of PDB 5zgt Chain B

Receptor sequence
>5zgtB (length=242) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
GEIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGL
IVRDGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGG
MDALHAAGIATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFG
PLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEH
YAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR
3D structure
PDB5zgt Active-Site Conformational Fluctuations Promote the Enzymatic Activity of NDM-1.
ChainB
Resolution1.2 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) H92 H94 D96 H161 C180 K183 N192 H222
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 B H120 H122 H189 H92 H94 H161
BS02 ZN B D124 C208 H250 D96 C180 H222
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:5zgt, PDBe:5zgt, PDBj:5zgt
PDBsum5zgt
PubMed30150473
UniProtC7C422|BLAN1_KLEPN Metallo-beta-lactamase type 2 (Gene Name=blaNDM-1)

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