Research workbench
Active site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase
Analyse Active site copper and zinc ions modulate the quaternary structure of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OAJ
- Type
- protein
- Length
- 151 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.73
- Source
- PHOTOBACTERIUM LEIOGNATHI
- Molecule
- Superoxide dismutase
- EC
- 1.15.1.1
- UniProt
- P00446
- Ligands
- ZN, CU
Structure
x-ray diffraction · resolution 1.73 · 1 distinct chain · 7% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase (EC 1.15.1.1) | protein | 151 | 7% helix, 39% strand | P00446 |
Ligands and binding sites
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
- 1OAJ · Active site copper and zinc ions modulate the quaternary structure of prokaryotic CU,ZN… · the same entry in another collection · chain A against A, TM-score 1.00
- P00446 · AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (P00446) · a predicted model of the same protein · 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 P00446
- Elsewhere: RCSB PDB 1OAJ · PDBe 1OAJ · UniProt P00446
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