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Structure of lactate oxidase at PH4.5 from aerococcus viridans

Analyse Structure of lactate oxidase at PH4.5 from aerococcus viridans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZFA
Type
protein
Length
681 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lactate oxidase
EC
1.13.12.4
UniProt
Q44467
Ligands
FMN
Pockets
10 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALactate oxidase (EC 1.13.12.4)protein35241% helix, 15% strandQ44467
BLactate oxidase (EC 1.13.12.4)protein32943% helix, 15% strandQ44467

Ligands and binding sites

  • FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11940.800.9434FMN, EDO
21980.790.9435FMN, EDO
3960.670.9121empty
43190.650.8143empty
5940.470.8117empty

Interfaces

1 interface between chains.

  • A–B · 1079 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 2ZFA · Structure of Lactate Oxidase at pH4.5 from AEROCOCCUS VIRIDANS · the same entry in another collection · chain A against A, TM-score 1.00

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