Research workbench
Crystal structure of human NEIL3 tandem zinc finger grf domains
Analyse Crystal structure of human NEIL3 tandem zinc finger grf domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JL5
- Type
- protein
- Length
- 178 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endonuclease 8-like 3
- EC
- 3.2.2.-, 4.2.99.18
- UniProt
- Q8TAT5
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endonuclease 8-like 3 (EC 3.2.2.-, 4.2.99.18) | protein | 88 | 7% helix, 30% strand | Q8TAT5 |
| B | Endonuclease 8-like 3 (EC 3.2.2.-, 4.2.99.18) | protein | 90 | 7% helix, 29% strand | Q8TAT5 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.40 | 0.76 | 23 | empty |
| 2 | 80 | 0.39 | 0.78 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 444 Ų buried · 9 hydrogen bonds · protein-protein
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 Q8TAT5
- Elsewhere: RCSB PDB 7JL5 · PDBe 7JL5 · UniProt Q8TAT5
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