Structure of PDB 2nyp Chain A

Receptor sequence
>2nypA (length=215) Species: 1396 (Bacillus cereus) [Search protein sequence]
TVIKNETGTISISQLNKNVWVHTELGVPSNGLVLNTSKGLVLVDSSWDDK
LTKELIEMVEKKFQKRVTDVIITHAHADHIGGIKTLKERGIKAHSTALTA
ELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQYN
ILVGGDLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGHGE
VGDKGLLLHTLDLLK
3D structure
PDB2nyp The Zn2 position in metallo-beta-lactamases is critical for activity: a study on chimeric metal sites on a conserved protein scaffold.
ChainA
Resolution1.84 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H86 H88 D90 H149 D168 K171 N180 H210
Catalytic site (residue number reindexed from 1) H74 H76 D78 H137 D156 K159 N168 H198
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 A H86 H88 H149 H74 H76 H137
BS02 ZN A H91 D168 H79 D156
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:2nyp, PDBe:2nyp, PDBj:2nyp
PDBsum2nyp
PubMed17915249
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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