MolNFT v1 · #159730 · protein
Crystal structure of the catalytic domain of human endonuclease V (C140S/C225S/C226A/C228S)
6OZE: “Crystal structure of the catalytic domain of human endonuclease V (C140S/C225S/C226A/C228S)”. X-ray diffraction, 1 ligand (NA), 1 pocket (best druggability 0.53). MolNFT v1 #159730 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6OZE
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endonuclease V
- EC
- 3.1.26.-
- UniProt
- Q8N8Q3
- Ligands
- NA
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endonuclease V (EC 3.1.26.-) | protein | 246 | 35% helix, 23% strand | Q8N8Q3 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 194 | 0.53 | 0.78 | 24 | 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 Q8N8Q3
- Elsewhere: RCSB PDB 6OZE · PDBe 6OZE · UniProt Q8N8Q3
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