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Crystal structure of human APOBEC3A
Analyse Crystal structure of human APOBEC3A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XXO
- Type
- protein
- Length
- 373 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA dc->du-editing enzyme apobec-3A
- EC
- 3.5.4.-
- UniProt
- P31941
- Ligands
- ZN, CL
- Pockets
- 5 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA dc->du-editing enzyme apobec-3A (EC 3.5.4.-) | protein | 186 | 35% helix, 22% strand | P31941 |
| B | DNA dc->du-editing enzyme apobec-3A (EC 3.5.4.-) | protein | 187 | 36% helix, 22% strand | P31941 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.57 | 0.79 | 31 | ZN, CL |
| 2 | 100 | 0.53 | 0.83 | 24 | ZN |
| 3 | 99 | 0.53 | 0.83 | 24 | ZN |
| 4 | 154 | 0.50 | 0.79 | 26 | empty |
| 5 | 118 | 0.47 | 0.79 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1082 Ų buried · 22 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 P31941
- Elsewhere: RCSB PDB 4XXO · PDBe 4XXO · UniProt P31941
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