Research workbench
REV1 UBM2 domain complex with ubiquitin
Analyse REV1 UBM2 domain complex with ubiquitin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ASR
- Type
- protein
- Length
- 189 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin; DNA repair protein REV1
- EC
- 2.7.7.-
- UniProt
- P0CG47, Q9UBZ9
- Ligands
- NI
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 3 distinct chains · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin | protein | 76 | 24% helix, 33% strand | P0CG47 |
| B | DNA repair protein REV1 (EC 2.7.7.-) | protein | 39 | 67% helix, 0% strand | Q9UBZ9 |
| C | Ubiquitin | protein | 74 | 24% helix, 35% strand | P0CG47 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 4 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.49 | 0.82 | 15 | NI |
Interfaces
3 interfaces between chains.
- A–B · 851 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 358 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 173 Ų buried · 4 hydrogen bonds · protein-protein
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 P0CG47
- Every structure of UniProt Q9UBZ9
- Elsewhere: RCSB PDB 6ASR · PDBe 6ASR · UniProt P0CG47 · UniProt Q9UBZ9
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