Research workbench
Native human manganese superoxide dismutase
Analyse Native human manganese superoxide dismutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VF9
- Type
- protein
- Length
- 398 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [mn], mitochondrial
- EC
- 1.15.1.1
- UniProt
- P04179
- Ligands
- MN, K, PO4
- Pockets
- 2 · best druggability 0.29
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Superoxide dismutase [mn], mitochondrial (EC 1.15.1.1) | protein | 199 | 58% helix, 13% strand | P04179 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- K · Potassium ion · metal · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.29 | 0.73 | 19 | PO4 |
| 2 | 55 | 0.27 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1091 Ų buried · 6 hydrogen bonds · protein-protein
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 P04179
- Elsewhere: RCSB PDB 5VF9 · PDBe 5VF9 · UniProt P04179
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