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Crystal structure of ampc ENT385 free form

Analyse Crystal structure of ampc ENT385 free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LC7
Type
protein
Length
705 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-lactamase
EC
3.5.2.6
Ligands
SO4
Pockets
7 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-lactamase (EC 3.5.2.6)protein35838% helix, 23% strand—
BBeta-lactamase (EC 3.5.2.6)protein34740% helix, 23% strand—

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 10 copies · chains A, B
  • GOL · Glycerol · additive · 7 copies · chains A, B
  • DIO · 1,4-diethylene dioxide · additive · 2 copies · chains B

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

Pockets

7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15380.640.7663GOL, SO4
21300.440.7631empty
31450.420.7429GOL
4850.400.7814GOL
5960.350.7428SO4

Interfaces

1 interface between chains.

  • A–B · 715 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 6LC7 · Crystal structure of AmpC Ent385 free form · the same entry in another collection · chain A against A, TM-score 1.00

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