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Crystal structure of human mitochondrial enolase superfamily member 1 (ENOSF1)

Analyse Crystal structure of human mitochondrial enolase superfamily member 1 (ENOSF1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4A35
Type
protein
Length
441 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mitochondrial enolase superfamily member 1
EC
5.-.-.-
UniProt
Q7L5Y1
Ligands
MG
Pockets
1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMitochondrial enolase superfamily member 1 (EC 5.-.-.-)protein44146% helix, 15% strandQ7L5Y1

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A
  • EDO · 1,2-ethanediol · additive · 7 copies · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11650.670.8734empty

Compared structures

  • 4A35 · Crystal structure of human Mitochondrial enolase superfamily member 1 (ENOSF1) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q7L5Y1 · AlphaFold monomer V2.0 prediction for mitochondrial enolase superfamily member 1 (Q7L5Y1) · a predicted model of the same protein · chain A against A, TM-score 0.99

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