MolNFT v1 · #20790 · protein
Structure of ERO1P, source of disulfide bonds for oxidative protein folding in the cell
1RQ1 · 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
- 1RQ1
- Type
- protein
- Length
- 356 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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical 65.0 kda protein in COX14-COS3 intergenic region precursor | protein | 356 | 57% helix, 6% strand | Q03103 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 241 | 0.70 | 0.86 | 37 | FAD |
| 2 | 415 | 0.60 | 0.75 | 36 | empty |
| 3 | 108 | 0.45 | 0.79 | 18 | CD |
| 4 | 83 | 0.42 | 0.79 | 15 | empty |
| 5 | 63 | 0.40 | 0.80 | 18 | empty |
Modifications
Observed in the structure: 5 disulfide, 1 covalent (disulfide, covalent ligand).
Compared structures
- 1RQ1 · 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 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q03103
- Elsewhere: RCSB PDB 1RQ1 · PDBe 1RQ1 · UniProt Q03103
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