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Catechol 2,3-dioxygenase (C23O64) from diaphorobacter sp DS2

Analyse Catechol 2,3-dioxygenase (C23O64) from diaphorobacter sp DS2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ZSZ
Type
protein
Length
293 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Catechol 2,3-dioxygenase, extradiol ring cleavage protein
EC
1.13.11.2
Ligands
CA, FE
Pockets
2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACatechol 2,3-dioxygenase, extradiol ring cleavage protein (EC 1.13.11.2)protein29317% helix, 40% strand—

Ligands and binding sites

  • CA · Calcium ion · metal · chains A
  • FE · Fe (III) ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1940.550.8520empty
2900.440.7918empty

Compared structures

  • 5ZSZ · Catechol 2,3-dioxygenase (C23O64) from Diaphorobacter sp DS2 · the same entry in another collection · chain A against A, TM-score 1.00

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