MolNFT v1 · #121489 · protein
APOBEC3F catalytic domain crystal structure
5HX5 · DNA dc->du-editing enzyme apobec-3F: “APOBEC3F catalytic domain crystal structure”. X-ray diffraction, 1 ligand (ZN), 4 pockets (best druggability 0.67). MolNFT v1 #121489 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5HX5
- Type
- protein
- Length
- 342 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA dc->du-editing enzyme apobec-3F
- EC
- 3.5.4.-
- UniProt
- Q8IUX4
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA dc->du-editing enzyme apobec-3F (EC 3.5.4.-) | protein | 174 | 43% helix, 25% strand | Q8IUX4 |
| B | DNA dc->du-editing enzyme apobec-3F (EC 3.5.4.-) | protein | 168 | 42% helix, 24% strand | Q8IUX4 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 605 | 0.67 | 0.77 | 58 | empty |
| 2 | 84 | 0.42 | 0.79 | 19 | empty |
| 3 | 80 | 0.37 | 0.77 | 16 | empty |
| 4 | 88 | 0.35 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 403 Ų buried · 3 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 Q8IUX4
- Elsewhere: RCSB PDB 5HX5 · PDBe 5HX5 · UniProt Q8IUX4
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