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Crystal structure of werner syndrome helicase
Analyse Crystal structure of werner syndrome helicase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YHR
- Type
- protein
- Length
- 541 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Werner syndrome ATP-dependent helicase
- EC
- 3.6.4.12, 3.1.-.-
- UniProt
- Q14191
- Ligands
- ADP, ZN
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Werner syndrome ATP-dependent helicase (EC 3.6.4.12, 3.1.-.-) | protein | 541 | 43% helix, 16% strand | Q14191 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 926 | 0.79 | 0.81 | 84 | ADP |
| 2 | 69 | 0.33 | 0.76 | 20 | empty |
| 3 | 82 | 0.32 | 0.73 | 16 | empty |
| 4 | 54 | 0.28 | 0.74 | 13 | empty |
| 5 | 52 | 0.25 | 0.73 | 12 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q14191
- Elsewhere: RCSB PDB 6YHR · PDBe 6YHR · UniProt Q14191
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