MolNFT v1 · #16984 · protein
Zn HIS46ARG mutant of human cu, zn superoxide dismutase
1OEZ · Superoxide dismutase [cu-zn]: “Zn HIS46ARG mutant of human cu, zn superoxide dismutase”. X-ray diffraction, 2 ligands (ZN, SO4), 5 pockets (best druggability 0.77). MolNFT v1 #16984 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1OEZ
- Type
- protein
- Length
- 496 residues
- Chains
- 4
- 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
- ZN, SO4
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| W, X, Y, Z | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 124 | 4% helix, 48% strand | P00441 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains W, X, Y, Z
- SO4 · Sulfate ion · ion · 4 copies · chains W, X, Y, Z
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1011 | 0.77 | 0.79 | 113 | empty |
| 2 | 91 | 0.42 | 0.79 | 22 | empty |
| 3 | 106 | 0.38 | 0.75 | 24 | empty |
| 4 | 102 | 0.33 | 0.73 | 19 | empty |
| 5 | 82 | 0.31 | 0.73 | 18 | empty |
Interfaces
4 interfaces between chains.
- W–X · 684 Ų buried · 4 hydrogen bonds · protein-protein
- Y–Z · 677 Ų buried · 4 hydrogen bonds · protein-protein
- X–Y · 317 Ų buried · 2 hydrogen bonds · protein-protein
- W–Z · 315 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1OEZ · Zn His46Arg mutant of Human Cu, Zn Superoxide Dismutase · the same entry in another collection · chain W against W, 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 1OEZ · PDBe 1OEZ · UniProt P00441
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