MolNFT v1 · #181480 · protein
Human exonuclease 5 crystal structure
7LW7 · Exonuclease V: “Human exonuclease 5 crystal structure”. X-ray diffraction, 1 ligand (SF4), 6 pockets (best druggability 0.57). MolNFT v1 #181480 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7LW7
- Type
- protein
- Length
- 277 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exonuclease V
- EC
- 3.1.-.-
- UniProt
- Q9H790
- Ligands
- SF4
- Pockets
- 6 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exonuclease V (EC 3.1.-.-) | protein | 277 | 47% helix, 17% strand | Q9H790 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
- EDO · 1,2-ethanediol · additive · 6 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 421 | 0.57 | 0.74 | 35 | EDO |
| 2 | 110 | 0.52 | 0.82 | 22 | empty |
| 3 | 77 | 0.36 | 0.76 | 16 | EDO |
| 4 | 75 | 0.35 | 0.75 | 11 | GOL |
| 5 | 55 | 0.32 | 0.77 | 15 | 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 Q9H790
- Elsewhere: RCSB PDB 7LW7 · PDBe 7LW7 · UniProt Q9H790
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