Structure of PDB 4rl2 Chain B

Receptor sequence
>4rl2B (length=241) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
EIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLI
VRDGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGM
DALHAAGIATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGP
LKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHY
AASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR
3D structure
PDB4rl2 Structural and Mechanistic Insights into NDM-1 Catalyzed Hydrolysis of Cephalosporins.
ChainB
Resolution2.008 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) H91 H93 D95 H160 C179 K182 N191 H221
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 3S3 B P68 G69 F70 P39 G40 F41
BS02 ZN B H120 H122 H189 H91 H93 H160
BS03 ZN B D124 C208 H250 D95 C179 H221
BS04 3S3 B L65 M67 W93 H122 Q123 D124 H189 C208 K211 G219 N220 H250 L36 M38 W64 H93 Q94 D95 H160 C179 K182 G190 N191 H221
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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Cellular Component
External links
PDB RCSB:4rl2, PDBe:4rl2, PDBj:4rl2
PDBsum4rl2
PubMed25268575
UniProtC7C422|BLAN1_KLEPN Metallo-beta-lactamase type 2 (Gene Name=blaNDM-1)

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