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MolNFT v1 · #129826 · protein

Crystal structure of an electron transfer flavoprotein from geobacter metallireducens

5OW0 · Electron transfer flavoprotein, beta subunit: “Crystal structure of an electron transfer flavoprotein from geobacter metallireducens”. X-ray diffraction, 2 ligands (AMP, FAD), 6 pockets (best druggability 0.77). MolNFT v1 #129826 on…

PDB
5OW0
Type
protein
Length
543 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Electron transfer flavoprotein, beta subunit; Electron transfer flavoprotein, alpha…
UniProt
Q39VG5, Q39VG4
Ligands
AMP, FAD
Pockets
6 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BElectron transfer flavoprotein, beta subunitprotein25131% helix, 31% strandQ39VG5
AElectron transfer flavoprotein, alpha subunitprotein29229% helix, 28% strandQ39VG4

Ligands and binding sites

  • AMP · Adenosine monophosphate · ligand · chains B
  • FAD · Flavin-adenine dinucleotide · ligand · chains B, A

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

Pockets

6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16220.770.8373empty
22440.760.8942AMP
33010.660.8242FAD
41590.570.8222empty
5970.560.8518empty

Interfaces

1 interface between chains.

  • B–A · 3596 Ų buried · 59 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

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