Structure of PDB 4rm5 Chain B

Receptor sequence
>4rm5B (length=222) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
DQRFGDLVFRQLAPNVWQHTSYLGAVASNGLIVRDGGRVLVVDTAWTDDQ
TAQILNWIKQEINLPVALAVVTHAHQNKMGGMDALHAAGIATYANALSNQ
LAPQEGMVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSDNITVG
IDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIV
MSHSAPDSRAAITHTARMADKL
3D structure
PDB4rm5 Structural and Mechanistic Insights into NDM-1 Catalyzed Hydrolysis of Cephalosporins.
ChainB
Resolution2.1 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 N124 H189 C208 K211 N220 H250
Catalytic site (residue number reindexed from 1) H73 H75 N77 H142 C161 K164 N173 H203
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 H73 H75 H142
BS02 ZN B C208 H250 C161 H203
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:4rm5, PDBe:4rm5, PDBj:4rm5
PDBsum4rm5
PubMed25268575
UniProtC7C422|BLAN1_KLEPN Metallo-beta-lactamase type 2 (Gene Name=blaNDM-1)

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