Research workbench
BORF2-APOBEC3BCTD complex
Analyse BORF2-APOBEC3BCTD complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RW6
- Type
- protein
- Length
- 1,634 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MALTOSE/MALTODEXTRIN-binding periplasmic protein, ribonucleoside-diphosphate reductase…
- EC
- 1.17.4.1, 3.5.4.38
- UniProt
- P03190, Q9UH17
- Ligands
- ZN
- Pockets
- 15 · best druggability 0.72
Structure
electron microscopy · 2 distinct chains · 44% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | MALTOSE/MALTODEXTRIN-binding periplasmic protein, ribonucleoside-diphosphate reductase large subunit (EC 1.17.4.1) | protein | 642 | 45% helix, 10% strand | P03190 |
| B, D | DNA dc->du-editing enzyme apobec-3B (EC 3.5.4.38) | protein | 175 | 39% helix, 18% strand | Q9UH17 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 741 | 0.72 | 0.78 | 79 | empty |
| 2 | 340 | 0.60 | 0.77 | 43 | empty |
| 3 | 348 | 0.59 | 0.77 | 36 | empty |
| 4 | 328 | 0.59 | 0.77 | 43 | empty |
| 5 | 214 | 0.58 | 0.80 | 27 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1183 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1174 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 844 Ų buried · 7 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 P03190
- Every structure of UniProt Q9UH17
- Elsewhere: RCSB PDB 7RW6 · PDBe 7RW6 · UniProt P03190 · UniProt Q9UH17
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