Research workbench
Structure of the Crb2-BRCT2 domain complex with phosphopeptide.
Analyse Structure of the Crb2-BRCT2 domain complex with phosphopeptide. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VXC
- Type
- protein
- Length
- 458 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.1
- Source
- SCHIZOSACCHAROMYCES POMBE; SYNTHETIC CONSTRUCT
- Molecule
- DNA repair protein RHP9; H2A1 peptide
- UniProt
- P87074
- Ligands
- PR
- Pockets
- 6 · best druggability 0.41
Structure
x-ray diffraction · resolution 3.1 · 3 distinct chains · 30% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair protein RHP9 | protein | 223 | 30% helix, 19% strand | P87074 |
| B | DNA repair protein RHP9 | protein | 231 | 29% helix, 19% strand | P87074 |
| C | H2A1 peptide | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
- PR · Praseodymium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.41 | 0.74 | 21 | empty |
| 2 | 50 | 0.39 | 0.81 | 14 | empty |
| 3 | 60 | 0.33 | 0.77 | 19 | empty |
| 4 | 76 | 0.33 | 0.75 | 17 | empty |
| 5 | 60 | 0.30 | 0.75 | 16 | empty |
Interfaces
2 interfaces between chains.
- A–B · 966 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 352 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, phosphorylation).
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 P87074
- Elsewhere: RCSB PDB 2VXC · PDBe 2VXC · UniProt P87074
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