MolNFT v1 · #43994 · protein
Structure and chemical shifts of CU(I),ZN(II) superoxide dismutase by solid-state NMR
2LU5 · Superoxide dismutase [cu-zn]: “Structure and chemical shifts of CU(I),ZN(II) superoxide dismutase by solid-state NMR”. Solid-state nmr, 1 ligand (CU). MolNFT v1 #43994 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2LU5
- Type
- protein
- Length
- 153 residues
- Chains
- 1
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [cu-zn]
- EC
- 1.15.1.1
- UniProt
- P00441
- Ligands
- CU
Structure
solid-state nmr · 1 distinct chain · 4% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 153 | 4% helix, 18% strand | P00441 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 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
- 2LU5 · Structure and chemical shifts of Cu(I),Zn(II) superoxide dismutase by solid-state NMR · 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 P00441
- Elsewhere: RCSB PDB 2LU5 · PDBe 2LU5 · UniProt P00441
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