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Structure of a lao-binding protein mutant with glutamine

Analyse Structure of a lao-binding protein mutant with glutamine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5OWF
Type
protein
Length
235 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
LYSINE/ARGININE/ORNITHINE-binding periplasmic protein
UniProt
P02911
Ligands
GLN
Pockets
1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALYSINE/ARGININE/ORNITHINE-binding periplasmic proteinprotein23538% helix, 23% strandP02911

Ligands and binding sites

  • GLN · Glutamine · ligand · chains A
  • EDO · 1,2-ethanediol · additive · 18 copies · chains A
  • GOL · Glycerol · additive · 2 copies · chains A
  • PEG · Di(hydroxyethyl)ether · 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
1850.350.7519EDO, GOL

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 5OWF · Structure of a LAO-binding protein mutant with glutamine · the same entry in another collection · chain A against A, TM-score 1.00
  • P02911 · AlphaFold monomer V2.0 prediction for LYSINE/ARGININE/ORNITHINE- binding periplasmic… · a predicted model of the same protein · chain A against A, TM-score 1.00

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