Research workbench
Crystal structure of bovine cu zn sod - (1 of 3)
Analyse Crystal structure of bovine cu zn sod - (1 of 3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E9Q
- Type
- protein
- Length
- 302 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase
- EC
- 1.13.1.1
- UniProt
- P00442
- Ligands
- CU, ZN
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase (EC 1.13.1.1) | protein | 151 | 6% helix, 42% strand | P00442 |
| B | Superoxide dismutase (EC 1.13.1.1) | protein | 151 | 6% helix, 42% strand | P00442 |
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 | 182 | 0.60 | 0.83 | 30 | empty |
| 2 | 92 | 0.34 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 692 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 P00442
- Elsewhere: RCSB PDB 1E9Q · PDBe 1E9Q · UniProt P00442
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