Research workbench
Crystal structure of wd-repeat domain of human WDR91
Analyse Crystal structure of wd-repeat domain of human WDR91 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VYC
- Type
- protein
- Length
- 661 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wd repeat-containing protein 91
- UniProt
- A4D1P6
- Ligands
- UNX
- Pockets
- 8 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Wd repeat-containing protein 91 | protein | 333 | 1% helix, 53% strand | A4D1P6 |
| B | Wd repeat-containing protein 91 | protein | 328 | 1% helix, 57% strand | A4D1P6 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 997 | 0.77 | 0.79 | 84 | empty |
| 2 | 629 | 0.75 | 0.81 | 48 | empty |
| 3 | 137 | 0.44 | 0.76 | 25 | empty |
| 4 | 99 | 0.39 | 0.76 | 17 | empty |
| 5 | 109 | 0.38 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 352 Ų buried · 4 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 A4D1P6
- Elsewhere: RCSB PDB 6VYC · PDBe 6VYC · UniProt A4D1P6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.