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MolNFT v1 · #20760 · protein

Structure of ERO1P, source of disulfide bonds for oxidative protein folding in the cell

1RP4 · Hypothetical 65.0 kda protein in COX14-COS3 intergenic…: “Structure of ERO1P, source of disulfide bonds for oxidative protein folding in the cell”. X-ray diffraction, 3 ligands (NEN, FAD, CD), 5 pockets (best druggability 0.70).…

PDB
1RP4
Type
protein
Length
374 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypothetical 65.0 kda protein in COX14-COS3 intergenic region precursor
UniProt
Q03103
Ligands
NEN, FAD, CD
Pockets
5 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHypothetical 65.0 kda protein in COX14-COS3 intergenic region precursorprotein37457% helix, 6% strandQ03103

Ligands and binding sites

  • NEN · 1-ethyl-pyrrolidine-2,5-dione · ligand · chains A
  • FAD · Flavin-adenine dinucleotide · ligand · chains A
  • CD · Cadmium ion · metal · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12140.700.8739FAD
24370.620.7633empty
31610.550.8122CD
41310.500.8025empty
5800.370.7619empty

Modifications

Observed in the structure: 7 modified, 5 disulfide, 1 covalent (engineered, disulfide, covalent ligand).

Compared structures

  • 1RP4 · Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell · the same entry in another collection · chain A against A, TM-score 1.00
  • Q03103 · AlphaFold monomer V2.0 prediction for endoplasmic oxidoreductin-1 (Q03103) · a predicted model of the same protein · chain A against A, TM-score 0.96

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