MolNFT v1 · #134400 · protein
Human mnsod-azide complex
5T30 · Superoxide dismutase [mn], mitochondrial: “Human mnsod-azide complex”. X-ray diffraction, 4 ligands (MN, K, PO4), 1 pocket (best druggability 0.25). MolNFT v1 #134400 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5T30
- 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, AZI
- Pockets
- 1 · best druggability 0.25
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 · 2 copies · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- AZI · Azide ion · ion · chains A
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 | 53 | 0.25 | 0.72 | 13 | PO4 |
Interfaces
1 interface between chains.
- A–B · 1094 Ų buried · 7 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 5T30 · PDBe 5T30 · UniProt P04179
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