Research workbench
Crystal structure analysis of the G73A mutant of superoxide dismutase from trichoderma reesei
Analyse Crystal structure analysis of the G73A mutant of 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
- 7SVS
- Type
- protein
- Length
- 1,562 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase
- EC
- 1.15.1.1
- UniProt
- G0RQS7
- Ligands
- MN
- Pockets
- 19 · best druggability 0.65
Structure
x-ray diffraction · 5 distinct chains · 58% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, H | Superoxide dismutase (EC 1.15.1.1) | protein | 196 | 60% helix, 13% strand | G0RQS7 |
| B, E | Superoxide dismutase (EC 1.15.1.1) | protein | 194 | 58% helix, 13% strand | G0RQS7 |
| C | Superoxide dismutase (EC 1.15.1.1) | protein | 202 | 57% helix, 12% strand | G0RQS7 |
| D, F | Superoxide dismutase (EC 1.15.1.1) | protein | 193 | 59% helix, 12% strand | G0RQS7 |
| G | Superoxide dismutase (EC 1.15.1.1) | protein | 194 | 59% helix, 13% strand | G0RQS7 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 432 | 0.65 | 0.78 | 58 | empty |
| 2 | 341 | 0.61 | 0.78 | 43 | empty |
| 3 | 156 | 0.60 | 0.84 | 24 | empty |
| 4 | 216 | 0.60 | 0.81 | 26 | empty |
| 5 | 152 | 0.59 | 0.83 | 23 | empty |
Interfaces
10 interfaces between chains.
- F–H · 1010 Ų buried · 2 hydrogen bonds · protein-protein
- E–G · 975 Ų buried · 3 hydrogen bonds · protein-protein
- A–F · 940 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 938 Ų buried · 9 hydrogen bonds · protein-protein
- B–E · 935 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 7SVS · Crystal structure analysis of the G73A mutant of Superoxide Dismutase from Trichoderma… · 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 G0RQS7
- Elsewhere: RCSB PDB 7SVS · PDBe 7SVS · UniProt G0RQS7
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