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Catechol oxidase from ipomoea batatas (sweet potatoes) in the native CU(II)-CU(II) state

Analyse Catechol oxidase from ipomoea batatas (sweet potatoes) in the native… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BT1
Type
protein
Length
672 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (catechol oxidase)
EC
1.10.3.1
UniProt
Q9ZP19
Ligands
C2O
Pockets
5 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BProtein (catechol oxidase) (EC 1.10.3.1)protein33638% helix, 7% strandQ9ZP19

Ligands and binding sites

  • C2O · Cu-O-Cu linkage · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12300.530.7620empty
2780.410.7920empty
3660.350.7720empty
4640.300.7512empty
5660.290.7313empty

Interfaces

1 interface between chains.

  • A–B · 349 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 1BT1 · Catechol oxidase from ipomoea batatas (sweet potatoes) in the native CU(II)-CU(II) state · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9ZP19 · AlphaFold monomer V2.0 prediction for polyphenol oxidase I, chloroplastic (Q9ZP19) · a predicted model of the same protein · chain A against A, TM-score 1.00

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