Research workbench
G152A mutant of mycobacterium tuberculosis iron-superoxide dismutase.
Analyse G152A mutant of mycobacterium tuberculosis iron-superoxide dismutase. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GN6
- Type
- protein
- Length
- 792 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase
- EC
- 1.15.1.1
- UniProt
- P17670
- Ligands
- FE
- Pockets
- 8 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Superoxide dismutase (EC 1.15.1.1) | protein | 198 | 57% helix, 13% strand | P17670 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 380 | 0.85 | 0.94 | 45 | empty |
| 2 | 771 | 0.72 | 0.78 | 85 | empty |
| 3 | 454 | 0.65 | 0.78 | 51 | empty |
| 4 | 302 | 0.61 | 0.79 | 38 | empty |
| 5 | 199 | 0.48 | 0.75 | 30 | empty |
Interfaces
6 interfaces between chains.
- A–C · 2264 Ų buried · 23 hydrogen bonds · protein-protein
- B–D · 2258 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 1002 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 981 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 210 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1GN6 · G152A mutant of Mycobacterium tuberculosis iron-superoxide dismutase. · 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 P17670
- Elsewhere: RCSB PDB 1GN6 · PDBe 1GN6 · UniProt P17670
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