Research workbench
Crystal structure of the copper chaperone for superoxide dismutase
Analyse Crystal structure of the copper chaperone for superoxide dismutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QUP
- Type
- protein
- Length
- 440 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P40202
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 221 | — | P40202 |
| B | — | protein | 219 | — | P40202 |
Compared structures
- 1QUP · Crystal structure of the copper chaperone for superoxide dismutase · the same entry in another collection · chain A against A, TM-score 1.00
- P40202 · AlphaFold monomer V2.0 prediction for superoxide dismutase 1 copper chaperone (P40202) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P40202
- Elsewhere: RCSB PDB 1QUP · PDBe 1QUP · UniProt P40202
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