Structure of PDB 4h0d Chain A

Receptor sequence
>4h0dA (length=241) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
AIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLI
VRDGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGM
DALHAAGIATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGP
LKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHY
AASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR
3D structure
PDB4h0d New Delhi Metallo-beta-Lactamase-1 Complexed with Mn from Klebsiella pneumoniae
ChainA
Resolution1.498 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 ZZ7 A M67 W93 H122 Q123 D124 H189 C208 K211 G219 N220 H250 M38 W64 H93 Q94 D95 H160 C179 K182 G190 N191 H221
BS02 MN A H120 H122 H189 H91 H93 H160
BS03 MN A D124 C208 H250 D95 C179 H221
BS04 MN A E227 H228 E198 H199
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:4h0d, PDBe:4h0d, PDBj:4h0d
PDBsum4h0d
PubMed
UniProtC7C422|BLAN1_KLEPN Metallo-beta-lactamase type 2 (Gene Name=blaNDM-1)

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