Research workbench
Crystal structure of human cu-zn superoxide dismutase mutant G85R in space group P21
Analyse Crystal structure of human cu-zn superoxide dismutase mutant G85R in space… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZKW
- Type
- protein
- Length
- 295 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
- P00441
- Ligands
- CU1, ZN
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 149 | 5% helix, 38% strand | P00441 |
| B | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 146 | 6% helix, 38% strand | P00441 |
Ligands and binding sites
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 | 144 | 0.61 | 0.85 | 27 | empty |
| 2 | 66 | 0.28 | 0.72 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 613 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2ZKW · Crystal structure of human Cu-Zn superoxide dismutase mutant G85R in space group P21 · 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 P00441
- Elsewhere: RCSB PDB 2ZKW · PDBe 2ZKW · UniProt P00441
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