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Crystal structure of coproporphyrinogen III oxidase

Analyse Crystal structure of coproporphyrinogen III oxidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TXN
Type
protein
Length
515 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Coproporphyrinogen III oxidase
EC
1.3.3.3
UniProt
P11353
Pockets
6 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACoproporphyrinogen III oxidase (EC 1.3.3.3)protein25938% helix, 27% strandP11353
BCoproporphyrinogen III oxidase (EC 1.3.3.3)protein25639% helix, 27% strandP11353

Ligands and binding sites

  • GOL · Glycerol · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111580.830.8587GOL
2970.490.8218empty
3860.450.8116empty
4600.430.8221empty
5520.340.7915empty

Interfaces

1 interface between chains.

  • A–B · 2943 Ų buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified, 1 disulfide (engineered, disulfide).

Compared structures

  • 1TXN · Crystal structure of coproporphyrinogen III oxidase · the same entry in another collection · chain A against A, TM-score 1.00
  • P11353 · AlphaFold monomer V2.0 prediction for oxygen-dependent coproporphyrinogen-III oxidase… · a predicted model of the same protein · chain B against A, TM-score 0.89

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