Research workbench
Inactive human ERO1
Analyse Inactive human ERO1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AHR
- Type
- protein
- Length
- 362 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ERO1-like protein alpha
- EC
- 1.8.4.-
- UniProt
- Q96HE7
- Ligands
- FAD
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ERO1-like protein alpha (EC 1.8.4.-) | protein | 362 | 58% helix, 8% strand | Q96HE7 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.74 | 0.90 | 32 | FAD |
| 2 | 513 | 0.66 | 0.77 | 54 | empty |
| 3 | 231 | 0.57 | 0.79 | 31 | empty |
| 4 | 139 | 0.51 | 0.79 | 21 | empty |
| 5 | 142 | 0.46 | 0.76 | 23 | empty |
Modifications
Observed in the structure: 6 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 Q96HE7
- Elsewhere: RCSB PDB 3AHR · PDBe 3AHR · UniProt Q96HE7
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