Research workbench
Curved pair of sheets formed from SOD1 residues 28-38 with familial mutation G37R.
Analyse Curved pair of sheets formed from SOD1 residues 28-38 with familial mutation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B79
- Type
- protein
- Length
- 22 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [cu-zn]
- EC
- 1.15.1.1
- UniProt
- P00441
- Ligands
- ORA
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 11 | 0% helix, 27% strand | P00441 |
Ligands and binding sites
- ORA · 7-hydroxy-8-[(E)-phenyldiazenyl]naphthalene-1,3-disulfonic acid · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 499 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 6B79 · Curved pair of sheets formed from SOD1 residues 28-38 with familial mutation G37R. · 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 6B79 · PDBe 6B79 · UniProt P00441
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