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Crystal structure of metallo beta lactamase from erythrobacter litoralis with beta mercaptoethanol in the active site

Analyse Crystal structure of metallo beta lactamase from erythrobacter litoralis with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6V73
Type
protein
Length
228 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-lactamase II
UniProt
Q2N9N3
Ligands
ZN, CL
Pockets
1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-lactamase IIprotein22829% helix, 27% strandQ2N9N3

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A
  • CL · Chloride ion · ion · chains A
  • BME · Beta-mercaptoethanol · additive · chains A
  • FMT · Formic acid · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11140.390.7521ZN, BME

Compared structures

  • 6V73 · Crystal Structure of Metallo Beta Lactamase from Erythrobacter litoralis with beta… · the same entry in another collection · chain A against A, TM-score 1.00

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