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MolNFT v1 · #5369 · protein

Three-dimensional structure of human electron transfer flavoprotein to 2.1 a resolution

1EFV: “Three-dimensional structure of human electron transfer flavoprotein to 2.1 a resolution”. X-ray diffraction, 2 ligands (FAD, AMP), 6 pockets (best druggability 0.83). MolNFT v1 #5369 on GenesisL1: 3D structure, binding sites and…

PDB
1EFV
Type
protein
Length
564 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Electron transfer flavoprotein
UniProt
P13804, P38117
Ligands
FAD, AMP
Pockets
6 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AElectron transfer flavoproteinprotein31232% helix, 30% strandP13804
BElectron transfer flavoproteinprotein25231% helix, 31% strandP38117

Ligands and binding sites

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

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

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16330.830.8759AMP
27990.770.8179empty
3560.650.9519empty
42660.580.7839empty
52460.580.7938FAD

Interfaces

1 interface between chains.

  • A–B · 3502 Ų buried · 57 hydrogen bonds · protein-protein

Compared structures

  • 1EFV · Three-dimensional structure of human electron transfer flavoprotein to 2.1 a resolution · the same entry in another collection · chain A against A, TM-score 1.00
  • P13804 · AlphaFold monomer V2.0 prediction for electron transfer flavoprotein subunit alpha… · a predicted model of the same protein · chain A against A, TM-score 1.00
  • P38117 · AlphaFold monomer V2.0 prediction for electron transfer flavoprotein subunit beta (P38117) · a predicted model of the same protein · chain B against A, TM-score 0.99

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