Research workbench
Metal-free tomato chloroplast superoxide dismutase
Analyse Metal-free tomato chloroplast superoxide dismutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HOG
- Type
- protein
- Length
- 127 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [cu-zn], chloroplastic
- EC
- 1.15.1.1
- UniProt
- P14831
- Ligands
- K
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [cu-zn], chloroplastic (EC 1.15.1.1) | protein | 127 | 4% helix, 46% strand | P14831 |
Ligands and binding sites
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3HOG · Metal-free Tomato Chloroplast Superoxide Dismutase · the same entry in another collection · chain A against A, TM-score 1.00
- P14831 · AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn], chloroplastic (P14831) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P14831
- Elsewhere: RCSB PDB 3HOG · PDBe 3HOG · UniProt P14831
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