MolNFT v1 · #36638 · protein
Wrn exonuclease, mg complex
2FBX · Werner syndrome helicase: “Wrn exonuclease, mg complex”. X-ray diffraction, 1 ligand (MG), 1 pocket (best druggability 0.39). MolNFT v1 #36638 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2FBX
- Type
- protein
- Length
- 195 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Werner syndrome helicase
- EC
- 2.7.7.-
- UniProt
- Q14191
- Ligands
- MG
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Werner syndrome helicase (EC 2.7.7.-) | protein | 195 | 42% helix, 18% strand | Q14191 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.39 | 0.74 | 24 | MG |
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 2FBX · PDBe 2FBX · UniProt Q14191
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