Research workbench
The 2.1 ångströms resolution structure of iron superoxide dismutase from pseudomonas ovalis
Analyse The 2.1 ångströms resolution structure of iron superoxide dismutase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SDP
- Type
- protein
- Length
- 372 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iron superoxide dismutase
- EC
- 1.15.1.1
- UniProt
- P09223
- Ligands
- FE
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Iron superoxide dismutase (EC 1.15.1.1) | protein | 186 | 30% helix, 3% strand | P09223 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 340 | 0.71 | 0.84 | 35 | empty |
| 2 | 307 | 0.67 | 0.82 | 27 | empty |
| 3 | 81 | 0.51 | 0.83 | 17 | empty |
| 4 | 62 | 0.32 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 968 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 3SDP · The 2.1 ångströms resolution structure of iron superoxide dismutase from pseudomonas… · the same entry in another collection · chain A against A, TM-score 1.00
- P09223 · AlphaFold monomer V2.0 prediction for superoxide dismutase [fe] (P09223) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P09223
- Elsewhere: RCSB PDB 3SDP · PDBe 3SDP · UniProt P09223
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