Research workbench
Crystal structure of Rev7-R124A/Rev3-RBM2 (residues 1988-2014) complex
Analyse Crystal structure of Rev7-R124A/Rev3-RBM2 (residues 1988-2014) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BC8
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.68
- Source
- Homo sapiens
- Molecule
- Mitotic spindle assembly checkpoint protein MAD2B; DNA polymerase zeta catalytic subunit
- EC
- 2.7.7.7
- UniProt
- Q9UI95, O60673
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · resolution 1.68 · 2 distinct chains · 34% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitotic spindle assembly checkpoint protein MAD2B | protein | 205 | 34% helix, 35% strand | Q9UI95 |
| B | DNA polymerase zeta catalytic subunit (EC 2.7.7.7) | protein | 25 | 36% helix, 24% strand | O60673 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.34 | 0.78 | 14 | ACT |
| 2 | 50 | 0.30 | 0.76 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1334 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 6BC8 · Crystal structure of REV7-R124A/REV3-RBM2 (residues 1988-2014) complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UI95 · AlphaFold monomer V2.0 prediction for mitotic spindle assembly checkpoint protein MAD2B… · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q9UI95
- Every structure of UniProt O60673
- Elsewhere: RCSB PDB 6BC8 · PDBe 6BC8 · UniProt Q9UI95 · UniProt O60673
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