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Crystal structure of metallo beta lactamase from hirschia baltica in complex with succinate

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

PDB
6V5M
Type
protein
Length
221 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-lactamase
EC
3.5.2.6
UniProt
C6XID6
Ligands
ZN
Pockets
1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-lactamase (EC 3.5.2.6)protein22125% helix, 29% strandC6XID6

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A
  • FMT · Formic acid · additive · 3 copies · chains A
  • SIN · Succinic acid · additive · 2 copies · chains A
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A
  • BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · 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
1790.360.7616ZN, SIN, EDO

Compared structures

  • 6V5M · Crystal Structure of Metallo Beta Lactamase from Hirschia baltica in Complex with… · the same entry in another collection · chain A against A, TM-score 1.00

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