Research workbench
Monomeric human sod mutant F50E/G51E/E133Q at atomic resolution
Analyse Monomeric human sod mutant F50E/G51E/E133Q at atomic resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MFM
- Type
- protein
- Length
- 153 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (COPPER,ZINC superoxide dismutase)
- EC
- 1.15.1.1
- UniProt
- P00441
- Ligands
- CD, ZN, CU, CL
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (COPPER,ZINC superoxide dismutase) (EC 1.15.1.1) | protein | 153 | 5% helix, 39% strand | P00441 |
Ligands and binding sites
- CD · Cadmium ion · metal · 9 copies · chains A
- ZN · Zinc ion · metal · chains A
- CU · Copper (II) ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · 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
- 1MFM · Monomeric human sod mutant F50E/G51E/E133Q at atomic resolution · 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 1MFM · PDBe 1MFM · UniProt P00441
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