Research workbench
Crystal structure of APOBEC3H
Analyse Crystal structure of APOBEC3H in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5W45
- Type
- protein
- Length
- 362 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- APOBEC3H
- UniProt
- B7TQM8
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | APOBEC3H | protein | 181 | 44% helix, 20% strand | B7TQM8 |
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
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1029 | 0.70 | 0.75 | 77 | empty |
| 2 | 119 | 0.43 | 0.77 | 23 | empty |
| 3 | 103 | 0.41 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 434 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 5W45 · Crystal structure of APOBEC3H · the same entry in another collection · chain A against A, TM-score 1.00
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 B7TQM8
- Elsewhere: RCSB PDB 5W45 · PDBe 5W45 · UniProt B7TQM8
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