MolNFT v1 · #146352 · protein
Structure of eremothecium gossypii SHU1:SHU2 complex
6DEX: “Structure of eremothecium gossypii SHU1:SHU2 complex”. X-ray diffraction, 2 ligands (MG, ZN). MolNFT v1 #146352 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6DEX
- Type
- protein
- Length
- 325 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q75DL0, Q74ZQ8
- Ligands
- MG, ZN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 130 | — | Q75DL0 |
| B | — | protein | 195 | — | 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.
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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