Research workbench
Crystal structure of the CU/ZN superoxide dismutase from cryptococcus liquefaciens strain N6
Analyse Crystal structure of the CU/ZN superoxide dismutase from cryptococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CE1
- Type
- protein
- Length
- 150 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [cu-zn]
- EC
- 1.15.1.1
- UniProt
- A0ZPR9
- Ligands
- ZN, CU
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 150 | 6% helix, 41% strand | A0ZPR9 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- CU · Copper (II) ion · metal · chains A
- ACT · Acetate ion · additive · 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
- 3CE1 · Crystal Structure of the Cu/Zn Superoxide Dismutase from Cryptococcus liquefaciens Strain… · 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 A0ZPR9
- Elsewhere: RCSB PDB 3CE1 · PDBe 3CE1 · UniProt A0ZPR9
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