Research workbench
Structure of the M305I mutant of cueo
Analyse Structure of the M305I 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
- 7F0V
- Type
- protein
- Length
- 949 residues
- Chains
- 2
- 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
- 9 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Blue copper oxidase cueo (EC 1.-.-.-) | protein | 475 | 12% helix, 40% strand | W8T2X0 |
| B | Blue copper oxidase cueo (EC 1.-.-.-) | protein | 474 | 11% helix, 42% strand | W8T2X0 |
Ligands and binding sites
- C2O · Cu-O-Cu linkage · ligand · 2 copies · chains A, B
- CU · Copper (II) ion · metal · 4 copies · chains A, B
- NO3 · Nitrate ion · ion · chains B
- PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1099 | 0.77 | 0.79 | 84 | empty |
| 2 | 60 | 0.51 | 0.86 | 19 | empty |
| 3 | 146 | 0.46 | 0.77 | 21 | empty |
| 4 | 134 | 0.45 | 0.77 | 23 | empty |
| 5 | 56 | 0.43 | 0.83 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 586 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7F0V · Structure of the M305I 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 7F0V · PDBe 7F0V · UniProt W8T2X0
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