MolNFT v1 · #96949 · protein
Crystal structure of the azide and iron substituted clostrium difficile SOD2 complex
4JYY · Superoxide dismutase: “Crystal structure of the azide and iron substituted clostrium difficile SOD2 complex”. X-ray diffraction, 2 ligands (FE, AZI), 1 pocket (best druggability 0.35). MolNFT v1 #96949 on GenesisL1: 3D structure…
- PDB
- 4JYY
- Type
- protein
- Length
- 202 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase
- EC
- 1.15.1.1
- UniProt
- Q186I6
- Ligands
- FE, AZI
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase (EC 1.15.1.1) | protein | 202 | 55% helix, 11% strand | Q186I6 |
Ligands and binding sites
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 | 94 | 0.35 | 0.74 | 20 | empty |
Compared structures
- 4JYY · Crystal structure of the azide and iron substituted Clostrium difficile SOD2 complex · the same entry in another collection · chain A against A, TM-score 1.00
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 Q186I6
- Elsewhere: RCSB PDB 4JYY · PDBe 4JYY · UniProt Q186I6
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