Research workbench
Crystal structure of the apo ATNUDT7
Analyse Crystal structure of the apo ATNUDT7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZB3
- Type
- protein
- Length
- 262 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nudix hydrolase 7
- EC
- 3.6.1.-, 3.6.1.13, 3.6.1.22
- UniProt
- Q9SU14
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nudix hydrolase 7 (EC 3.6.1.-, 3.6.1.13, 3.6.1.22) | protein | 262 | 25% helix, 35% strand | Q9SU14 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 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 | 221 | 0.59 | 0.80 | 28 | 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 Q9SU14
- Elsewhere: RCSB PDB 4ZB3 · PDBe 4ZB3 · UniProt Q9SU14
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.