Research workbench
CU/ZN superoxide dismutase from neisseria meningitidis K91E, K94E double mutant
Analyse CU/ZN superoxide dismutase from neisseria meningitidis K91E, K94E double mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AQS
- Type
- protein
- Length
- 315 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [cu-zn]
- EC
- 1.15.1.1
- UniProt
- Q59623
- Ligands
- CU1, ZN, CU
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 160 | 7% helix, 39% strand | Q59623 |
| B | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 155 | 7% helix, 40% strand | Q59623 |
Ligands and binding sites
- CU1 · Copper (I) ion · metal · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
- CU · Copper (II) ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.71 | 0.98 | 18 | empty |
| 2 | 65 | 0.26 | 0.72 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 955 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2AQS · CU/ZN superoxide dismutase from neisseria meningitidis K91E, K94E double mutant · the same entry in another collection · chain A against A, TM-score 1.00
- Q59623 · AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (Q59623) · 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 Q59623
- Elsewhere: RCSB PDB 2AQS · PDBe 2AQS · UniProt Q59623
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