MolNFT v1 · #16833 · protein
Active site copper and zinc ions modulate the quaternary structure of prokaryotic CU,ZN superoxide dismutase
1OAL: “Active site copper and zinc ions modulate the quaternary structure of prokaryotic CU,ZN superoxide dismutase”. X-ray diffraction, 2 ligands (ZN, CU). MolNFT v1 #16833 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1OAL
- Type
- protein
- Length
- 151 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase
- EC
- 1.15.1.1
- UniProt
- P00446
- Ligands
- ZN, CU
Structure
x-ray diffraction · 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
- 1OAL · 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 1OAL · PDBe 1OAL · UniProt P00446
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