Research workbench
CU/ZN superoxide dismutase from brucella abortus
Analyse CU/ZN superoxide dismutase from brucella abortus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L05
- Type
- protein
- Length
- 154 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
- P15453
- Ligands
- CU1, CU, ZN, SO4
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 154 | 7% helix, 44% strand | P15453 |
Ligands and binding sites
- CU1 · Copper (I) ion · metal · chains A
- CU · Copper (II) ion · metal · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · 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
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 P15453
- Elsewhere: RCSB PDB 4L05 · PDBe 4L05 · UniProt P15453
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