Research workbench
Structure-function in E. COLI iron superoxide dismutase: comparisons with the manganese enzyme from T. thermophilus
Analyse Structure-function in E. COLI iron superoxide dismutase: comparisons with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MNG
- Type
- protein
- Length
- 406 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Manganese superoxide dismutase
- EC
- 1.15.1.1
- UniProt
- P61503
- Ligands
- MN, AZI
- Pockets
- 4 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Manganese superoxide dismutase (EC 1.15.1.1) | protein | 203 | 57% helix, 10% strand | P61503 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- AZI · Azide ion · ion · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 170 | 0.51 | 0.78 | 21 | empty |
| 2 | 178 | 0.51 | 0.78 | 23 | empty |
| 3 | 100 | 0.37 | 0.75 | 24 | empty |
| 4 | 105 | 0.36 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 932 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1MNG · Structure-function in E. COLI iron superoxide dismutase: comparisons with the manganese… · the same entry in another collection · chain A against A, TM-score 1.00
- P61503 · AlphaFold monomer V2.0 prediction for superoxide dismutase [mn] (P61503) · a predicted model of the same protein · 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 P61503
- Elsewhere: RCSB PDB 1MNG · PDBe 1MNG · UniProt P61503
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