Research workbench
Multicopper oxidase cueo mutant C500SE506Q (DATA6)
Analyse Multicopper oxidase cueo mutant C500SE506Q (DATA6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UAE
- Type
- protein
- Length
- 476 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Blue copper oxidase cueo
- UniProt
- P36649
- Ligands
- CU, O
- Pockets
- 6 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Blue copper oxidase cueo | protein | 476 | 12% helix, 41% strand | P36649 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 3 copies · chains A
- O · Oxygen atom · ion · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.44 | 0.76 | 22 | empty |
| 2 | 52 | 0.42 | 0.83 | 17 | empty |
| 3 | 52 | 0.41 | 0.83 | 19 | empty |
| 4 | 84 | 0.40 | 0.78 | 20 | empty |
| 5 | 90 | 0.35 | 0.74 | 22 | empty |
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 P36649
- Elsewhere: RCSB PDB 3UAE · PDBe 3UAE · UniProt P36649
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