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Crystal structure of tla-3 extended-spectrum beta-lactamase

Analyse Crystal structure of tla-3 extended-spectrum beta-lactamase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5GS8
Type
protein
Length
275 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-lactamase
EC
3.5.2.6
UniProt
A0A0B6VPP7
Ligands
NA, SO4, CL
Pockets
1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-lactamase (EC 3.5.2.6)protein27546% helix, 20% strandA0A0B6VPP7

Ligands and binding sites

  • NA · Sodium ion · metal · 15 copies · chains A
  • SO4 · Sulfate ion · ion · 5 copies · chains A
  • CL · Chloride ion · ion · 2 copies · 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
11440.440.7622SO4

Compared structures

  • 5GS8 · Crystal structure of TLA-3 extended-spectrum beta-lactamase · the same entry in another collection · chain A against A, TM-score 1.00

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