Research workbench
Structure of eremothecium gossypii SHU1:SHU2 complex
Analyse Structure of eremothecium gossypii SHU1:SHU2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DEX
- Type
- protein
- Length
- 325 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Suppressor of hydroxyurea sensitivity protein 1; Suppressor of hydroxyurea sensitivity…
- UniProt
- Q75DL0, Q74ZQ8
- Ligands
- MG, ZN
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Suppressor of hydroxyurea sensitivity protein 1 | protein | 130 | 54% helix, 17% strand | Q75DL0 |
| B | Suppressor of hydroxyurea sensitivity protein 2 | protein | 195 | 40% helix, 16% strand | Q74ZQ8 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- ZN · Zinc ion · metal · chains B
- NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · chains A, B
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 | 189 | 0.49 | 0.76 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 1503 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 6DEX · Structure of Eremothecium gossypii Shu1:Shu2 complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q74ZQ8 · AlphaFold monomer V2.0 prediction for suppressor of hydroxyurea sensitivity protein 2… · a predicted model of the same protein · chain B against A, TM-score 0.95
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 Q75DL0
- Every structure of UniProt Q74ZQ8
- Elsewhere: RCSB PDB 6DEX · PDBe 6DEX · UniProt Q75DL0 · UniProt Q74ZQ8
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