Research workbench
Structure of ERO1P, source of disulfide bonds for oxidative protein folding in the cell
Analyse Structure of ERO1P, source of disulfide bonds for oxidative protein folding in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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