MolNFT v1 · #37106 · protein
Crystal structures of E. COLI laccase cueo under different copper binding situations
2FQG · Blue copper oxidase cueo: “Crystal structures of E. COLI laccase cueo under different copper binding situations”. X-ray diffraction, 3 ligands (C2O, CU, NA), 3 pockets (best druggability 0.42). MolNFT v1 #37106 on GenesisL1: 3D…
- PDB
- 2FQG
- Type
- protein
- Length
- 464 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
- 3 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Blue copper oxidase cueo (EC 1.-.-.-) | protein | 464 | 11% 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 · 2 copies · chains A
- CIT · Citric acid · additive · chains A
- PGE · Triethylene glycol · additive · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.42 | 0.79 | 23 | CIT |
| 2 | 111 | 0.40 | 0.76 | 22 | empty |
| 3 | 69 | 0.29 | 0.73 | 19 | empty |
Compared structures
- 2FQG · 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 2FQG · PDBe 2FQG · UniProt P36649
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