Research workbench
15 atmosphere oxygen yeast CU/ZN superoxide dismutase room temperature (298K) structure
Analyse 15 atmosphere oxygen yeast CU/ZN superoxide dismutase room temperature (298K)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B4L
- Type
- protein
- Length
- 153 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (CU/ZN superoxide dismutase)
- EC
- 1.15.1.1
- UniProt
- P00445
- Ligands
- CU, ZN
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (CU/ZN superoxide dismutase) (EC 1.15.1.1) | protein | 153 | 5% helix, 37% strand | P00445 |
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
- 1B4L · 15 atmosphere oxygen yeast CU/ZN superoxide dismutase room temperature (298K) structure · the same entry in another collection · chain A against A, TM-score 1.00
- P00445 · AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (P00445) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00445
- Elsewhere: RCSB PDB 1B4L · PDBe 1B4L · UniProt P00445
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