GL1X · GenesisL1 explorer

MolNFT v1 · #35109 · protein

Crystal structure of L-glutamate oxidase from streptomyces sp. X-119-6

2E1M: “Crystal structure of L-glutamate oxidase from streptomyces sp. X-119-6”. X-ray diffraction, 2 ligands (FAD, PO4), 10 pockets (best druggability 0.87). MolNFT v1 #35109 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
2E1M
Type
protein
Length
597 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-glutamate oxidase
EC
1.4.3.11
UniProt
Q8L3C7
Ligands
FAD, PO4
Pockets
10 · best druggability 0.87

Structure

x-ray diffraction · 3 distinct chains · 36% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AL-glutamate oxidase (EC 1.4.3.11)protein35636% helix, 20% strandQ8L3C7
BL-glutamate oxidase (EC 1.4.3.11)protein9039% helix, 24% strandQ8L3C7
CL-glutamate oxidase (EC 1.4.3.11)protein15135% helix, 21% strandQ8L3C7

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · chains A, B, C
  • PO4 · Phosphate ion · ion · 3 copies · chains A, C

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

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111860.870.88117FAD
21900.800.9531empty
3550.520.8713empty
41630.460.7623empty
52010.460.7435PO4

Interfaces

3 interfaces between chains.

  • A–C · 4015 Ų buried · 60 hydrogen bonds · protein-protein
  • B–C · 3409 Ų buried · 66 hydrogen bonds · protein-protein
  • A–B · 1771 Ų buried · 34 hydrogen bonds · protein-protein

Compared structures

  • 2E1M · Crystal Structure of L-Glutamate Oxidase from Streptomyces sp. X-119-6 · the same entry in another collection · chain A against A, TM-score 1.00

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