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Structure of the CRB2-BRCT2 domain
Analyse Structure of the CRB2-BRCT2 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VXB
- Type
- protein
- Length
- 449 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair protein RHP9
- UniProt
- P87074
- Ligands
- PR
- Pockets
- 4 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair protein RHP9 | protein | 225 | 31% helix, 17% strand | P87074 |
| B | DNA repair protein RHP9 | protein | 224 | 31% helix, 20% strand | P87074 |
Ligands and binding sites
- PR · Praseodymium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.45 | 0.75 | 30 | empty |
| 2 | 152 | 0.45 | 0.76 | 27 | empty |
| 3 | 56 | 0.34 | 0.77 | 13 | empty |
| 4 | 61 | 0.30 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 950 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 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 P87074
- Elsewhere: RCSB PDB 2VXB · PDBe 2VXB · UniProt P87074
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