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Crystal structure of ERV2P
Analyse Crystal structure of ERV2P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JR8
- Type
- protein
- Length
- 210 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ERV2 protein, mitochondrial
- UniProt
- Q12284
- Ligands
- FAD
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ERV2 protein, mitochondrial | protein | 105 | 69% helix, 0% strand | Q12284 |
| B | ERV2 protein, mitochondrial | protein | 105 | 70% helix, 0% strand | Q12284 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 248 | 0.65 | 0.82 | 30 | FAD |
| 2 | 275 | 0.65 | 0.81 | 42 | FAD |
| 3 | 85 | 0.37 | 0.76 | 14 | empty |
| 4 | 56 | 0.32 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1246 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 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 Q12284
- Elsewhere: RCSB PDB 1JR8 · PDBe 1JR8 · UniProt Q12284
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