Research workbench
The P212121 crystal structure of sodci superoxide dismutase with 2 molecules in the asymmetric unit at 1.7 a resolution
Analyse The P212121 crystal structure of sodci superoxide dismutase with 2 molecules in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VBT
- Type
- protein
- Length
- 310 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
- A0A0D6GQL3
- Ligands
- CU, ZN
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 156 | 7% helix, 39% strand | A0A0D6GQL3 |
| B | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 154 | 7% helix, 42% strand | A0A0D6GQL3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 811 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6VBT · The P212121 Crystal structure of SodCI Superoxide Dismutase with 2 molecules in the… · 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 A0A0D6GQL3
- Elsewhere: RCSB PDB 6VBT · PDBe 6VBT · UniProt A0A0D6GQL3
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