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Structure of 6-aminohexanoate-oligomer hydrolase from arthrobacter sp. KI72., D122V muntant

Analyse Structure of 6-aminohexanoate-oligomer hydrolase from arthrobacter sp. KI72.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5XYS
Type
protein
Length
663 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Endo-type 6-aminohexanoate oligomer hydrolase
UniProt
Q57326
Ligands
PO4
Pockets
4 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndo-type 6-aminohexanoate oligomer hydrolaseprotein33126% helix, 33% strandQ57326
BEndo-type 6-aminohexanoate oligomer hydrolaseprotein33226% helix, 33% strandQ57326

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 2 copies · chains A, B
  • GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1730.710.9628empty
26130.700.7874empty
3600.350.7819empty
4550.310.7614empty

Interfaces

1 interface between chains.

  • A–B · 1332 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 5XYS · Structure of 6-aminohexanoate-oligomer hydrolase from Arthrobacter sp. KI72., D122V mutant · the same entry in another collection · chain A against A, TM-score 1.00

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