MolNFT v1 · #44391 · protein
NMR structure of human restriction factor APOBEC3A
2M65 · Probable DNA dc->du-editing enzyme apobec-3A: “NMR structure of human restriction factor APOBEC3A”. Solution nmr, 1 ligand (ZN), 2 pockets (best druggability 0.71). MolNFT v1 #44391 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2M65
- Type
- protein
- Length
- 199 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable DNA dc->du-editing enzyme apobec-3A
- EC
- 3.5.4.-
- UniProt
- P31941
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.71
Structure
solution nmr · 1 distinct chain · 33% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable DNA dc->du-editing enzyme apobec-3A (EC 3.5.4.-) | protein | 199 | 33% helix, 21% strand | P31941 |
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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 206 | 0.71 | 0.87 | 38 | ZN |
| 2 | 55 | 0.30 | 0.76 | 17 | empty |
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 2M65 · PDBe 2M65 · UniProt P31941
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