MolNFT v1 · #15302 · protein
Catalytic and structural effects of amino-acid substitution at HIS30 in human manganese superoxide dismutase
1N0N · Superoxide dismutase [mn]: “Catalytic and structural effects of amino-acid substitution at HIS30 in human manganese superoxide dismutase”. X-ray diffraction, 2 ligands (MN, SO4), 1 pocket (best druggability 0.27). MolNFT v1 #15302…
- PDB
- 1N0N
- Type
- protein
- Length
- 396 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [mn]
- EC
- 1.15.1.1
- UniProt
- P04179
- Ligands
- MN, SO4
- Pockets
- 1 · best druggability 0.27
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Superoxide dismutase [mn] (EC 1.15.1.1) | protein | 198 | 58% helix, 13% strand | P04179 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.27 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 979 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1N0N · Catalytic and Structural Effects of Amino-Acid Substitution at His30 in Human Manganese… · the same entry in another collection · chain A against A, TM-score 1.00
- P04179 · AlphaFold monomer V2.0 prediction for superoxide dismutase [mn], mitochondrial (P04179) · a predicted model of the same protein · 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 P04179
- Elsewhere: RCSB PDB 1N0N · PDBe 1N0N · UniProt P04179
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