MolNFT v1 · #45730 · protein
NMR structure of the C-terminal domain of human APOBEC3B
2NBQ · DNA dc->du-editing enzyme apobec-3B: “NMR structure of the C-terminal domain of human APOBEC3B”. Solution nmr, 1 ligand (ZN), 3 pockets (best druggability 0.41). MolNFT v1 #45730 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 2NBQ
- Type
- protein
- Length
- 197 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA dc->du-editing enzyme apobec-3B
- EC
- 3.5.4.-
- UniProt
- Q9UH17
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.41
Structure
solution nmr · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA dc->du-editing enzyme apobec-3B (EC 3.5.4.-) | protein | 197 | 40% helix, 17% strand | Q9UH17 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.41 | 0.78 | 15 | empty |
| 2 | 87 | 0.38 | 0.76 | 16 | empty |
| 3 | 62 | 0.29 | 0.74 | 17 | empty |
Compared structures
- 2NBQ · NMR Structure of the C-Terminal Domain of human APOBEC3B · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UH17 · AlphaFold monomer V2.0 prediction for DNA dc->du-editing enzyme apobec-3B (Q9UH17) · a predicted model of the same protein · chain A against A, TM-score 0.85
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 Q9UH17
- Elsewhere: RCSB PDB 2NBQ · PDBe 2NBQ · UniProt Q9UH17
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.