Research workbench
Structure of blm rqc domain bound to a phosphate ion
Analyse Structure of blm rqc domain bound to a phosphate ion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WE2
- Type
- protein
- Length
- 233 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bloom syndrome protein
- EC
- 3.6.4.12
- UniProt
- P54132
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bloom syndrome protein (EC 3.6.4.12) | protein | 121 | 36% helix, 17% strand | P54132 |
| B | Bloom syndrome protein (EC 3.6.4.12) | protein | 112 | 38% helix, 18% strand | P54132 |
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 | 135 | 0.47 | 0.78 | 23 | PO4 |
| 2 | 68 | 0.41 | 0.81 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 345 Ų buried · 2 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 P54132
- Elsewhere: RCSB PDB 3WE2 · PDBe 3WE2 · UniProt P54132
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