MolNFT v1 · #113512 · protein
Crystal structure of human 5' exonuclease apollo
5AHO: “Crystal structure of human 5' exonuclease apollo”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.62). MolNFT v1 #113512 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5AHO
- Type
- protein
- Length
- 314 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5' exonuclease apollo
- EC
- 3.1.-.-
- UniProt
- Q9H816
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5' exonuclease apollo (EC 3.1.-.-) | protein | 314 | 27% helix, 24% strand | Q9H816 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 6 copies · chains A
- TLA · L(+)-tartaric acid · additive · 2 copies · 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 | 297 | 0.62 | 0.80 | 44 | TLA, EDO |
| 2 | 109 | 0.36 | 0.74 | 22 | EDO |
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 Q9H816
- Elsewhere: RCSB PDB 5AHO · PDBe 5AHO · UniProt Q9H816
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