Research workbench
Crystal structures of E. COLI laccase cueo under different copper binding situations
Analyse Crystal structures of E. COLI laccase cueo under different copper binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FQE
- Type
- protein
- Length
- 463 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Blue copper oxidase cueo
- EC
- 1.-.-.-
- UniProt
- P36649
- Ligands
- C2O, CU, NA
- Pockets
- 4 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Blue copper oxidase cueo (EC 1.-.-.-) | protein | 463 | 12% helix, 42% strand | P36649 |
Ligands and binding sites
- C2O · Cu-O-Cu linkage · ligand · chains A
- CU · Copper (II) ion · metal · 2 copies · chains A
- NA · Sodium ion · metal · chains A
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.42 | 0.79 | 26 | CIT |
| 2 | 113 | 0.41 | 0.76 | 21 | empty |
| 3 | 50 | 0.36 | 0.80 | 15 | empty |
| 4 | 64 | 0.30 | 0.74 | 19 | empty |
Compared structures
- 2FQE · Crystal Structures of E. coli Laccase CueO under different copper binding situations · the same entry in another collection · chain A against A, TM-score 1.00
- P36649 · AlphaFold monomer V2.0 prediction for blue copper oxidase cueo (P36649) · a predicted model of the same protein · 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 P36649
- Elsewhere: RCSB PDB 2FQE · PDBe 2FQE · UniProt P36649
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