Structure of PDB 6mgy Chain B

Receptor sequence
>6mgyB (length=226) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
GDQRFGDLVFRQLAPNVWQHTSYLDMGAVASNGLIVRDGGRVLLVDTAWT
DDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYANAL
SNQLAPQEGLVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSDNI
TVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKAS
MIVMSHSAPDSRAAITHTARMADKLR
3D structure
PDB6mgy Crystal Structure of the New Deli Metallo Beta Lactamase Variant 5 from Klebsiella pneumoniae
ChainB
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) H120 H122 D124 H189 C208 K211 N220 H250
Catalytic site (residue number reindexed from 1) H76 H78 D80 H145 C164 K167 N176 H206
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 H76 H78 H145
BS02 ZN B D124 C208 H250 D80 C164 H206
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:6mgy, PDBe:6mgy, PDBj:6mgy
PDBsum6mgy
PubMed
UniProtC7C422|BLAN1_KLEPN Metallo-beta-lactamase type 2 (Gene Name=blaNDM-1)

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