Research workbench
Structure of the human nocturnin catalytic domain with bound sulfate anion
Analyse Structure of the human nocturnin catalytic domain with bound sulfate anion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BT2
- Type
- protein
- Length
- 541 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nocturnin
- EC
- 3.1.13.4
- UniProt
- Q9UK39
- Ligands
- MG, SO4
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nocturnin (EC 3.1.13.4) | protein | 270 | 23% helix, 35% strand | Q9UK39 |
| B | Nocturnin (EC 3.1.13.4) | protein | 271 | 25% helix, 35% strand | Q9UK39 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 637 | 0.73 | 0.80 | 61 | empty |
| 2 | 52 | 0.37 | 0.79 | 11 | empty |
| 3 | 83 | 0.31 | 0.73 | 21 | MG, SO4 |
| 4 | 53 | 0.27 | 0.74 | 18 | MG, SO4 |
Interfaces
1 interface between chains.
- A–B · 385 Ų buried · 2 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 Q9UK39
- Elsewhere: RCSB PDB 6BT2 · PDBe 6BT2 · UniProt Q9UK39
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