Research workbench
Structure of the G304E mutant of cueo
Analyse Structure of the G304E mutant of cueo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F19
- Type
- protein
- Length
- 444 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Blue copper oxidase cueo
- EC
- 1.-.-.-
- UniProt
- W8T2X0
- Ligands
- C2O, CU, NO3
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Blue copper oxidase cueo (EC 1.-.-.-) | protein | 444 | 7% helix, 44% strand | W8T2X0 |
Ligands and binding sites
- C2O · Cu-O-Cu linkage · ligand · chains A
- CU · Copper (II) ion · metal · 2 copies · chains A
- NO3 · Nitrate ion · ion · 3 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.50 | 0.80 | 29 | empty |
| 2 | 117 | 0.41 | 0.76 | 22 | PEG |
| 3 | 52 | 0.31 | 0.77 | 15 | empty |
Compared structures
- 7F19 · Structure of the G304E mutant of CueO · 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 W8T2X0
- Elsewhere: RCSB PDB 7F19 · PDBe 7F19 · UniProt W8T2X0
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