Research workbench
Three-dimensional structure of xenopus laevis CU,ZN superoxide dismutase B determined by X-ray crystallography at 1.5 ångströms resolution
Analyse Three-dimensional structure of xenopus laevis CU,ZN superoxide dismutase B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XSO
- Type
- protein
- Length
- 300 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- COPPER,ZINC superoxide dismutase
- EC
- 1.15.1.1
- UniProt
- P15107
- Ligands
- CU, ZN
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | COPPER,ZINC superoxide dismutase (EC 1.15.1.1) | protein | 150 | 6% helix, 42% strand | P15107 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.56 | 0.79 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 677 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1XSO · Three-dimensional structure of xenopus laevis CU,ZN superoxide dismutase B determined by… · the same entry in another collection · chain A against A, TM-score 1.00
- P15107 · AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] B (P15107) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P15107
- Elsewhere: RCSB PDB 1XSO · PDBe 1XSO · UniProt P15107
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