Research workbench
Crystal structure of the C143A/C166A mutant of ERO1P
Analyse Crystal structure of the C143A/C166A mutant of ERO1P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NVJ
- Type
- protein
- Length
- 351 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoplasmic oxidoreductin-1
- EC
- 1.8.4.-
- UniProt
- Q03103
- Ligands
- NEN, FAD, CD
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoplasmic oxidoreductin-1 (EC 1.8.4.-) | protein | 351 | 60% 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 · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 262 | 0.72 | 0.86 | 34 | FAD |
| 2 | 147 | 0.52 | 0.80 | 23 | CD |
| 3 | 85 | 0.41 | 0.78 | 19 | empty |
| 4 | 66 | 0.37 | 0.78 | 20 | empty |
| 5 | 69 | 0.34 | 0.75 | 11 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
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 3NVJ · PDBe 3NVJ · UniProt Q03103
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