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Crystal structure of Acinetobacter baumannii OccAB1

Analyse Crystal structure of Acinetobacter baumannii OccAB1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DL5
Type
protein
Length
416 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.05
Source
Acinetobacter baumannii AB307-0294
Molecule
Membrane protein
UniProt
A0A0F5EN03
Ligands
PO4
Pockets
2 · best druggability 0.70

Structure

x-ray diffraction · resolution 2.05 · 1 distinct chain · 1% helix, 57% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMembrane proteinprotein4161% helix, 57% strandA0A0F5EN03

Ligands and binding sites

  • PO4 · Phosphate ion · ion · chains A
  • C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 3 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18820.700.7591C8E
2640.290.7315empty

Compared structures

  • 5DL5 · Crystal structure of acinetobacter baumannii OCCAB1 · the same entry in another collection · chain A against A, TM-score 1.00

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