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Solution structure of apo CU,ZN superoxide dismutase: role of metal ions in protein folding
Analyse Solution structure of apo CU,ZN superoxide dismutase: role of metal ions in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RK7
- Type
- protein
- Length
- 153 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [cu-zn]
- EC
- 1.15.1.1
- UniProt
- P00441
- Pockets
- 2 · best druggability 0.71
Structure
solution nmr · 1 distinct chain · 0% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 153 | 0% helix, 22% strand | P00441 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.71 | 0.91 | 33 | empty |
| 2 | 173 | 0.54 | 0.80 | 34 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1RK7 · Solution structure of apo Cu,Zn Superoxide Dismutase: role of metal ions in protein… · 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 1RK7 · PDBe 1RK7 · UniProt P00441
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