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The 1.58A crystal structure of human coproporphyrinogen oxidase reveals the structural basis of hereditary coproporphyria

Analyse The 1.58A crystal structure of human coproporphyrinogen oxidase reveals the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2AEX
Type
protein
Length
336 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Coproporphyrinogen III oxidase, mitochondrial
EC
1.3.3.3
UniProt
P36551
Pockets
4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACoproporphyrinogen III oxidase, mitochondrial (EC 1.3.3.3)protein33642% helix, 24% strandP36551

Ligands and binding sites

  • 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12170.760.9139CIT
21280.520.8021empty
3790.410.7922empty
4530.350.7914empty

Compared structures

  • 2AEX · The 1.58A Crystal Structure of Human Coproporphyrinogen Oxidase Reveals the Structural… · the same entry in another collection · chain A against A, TM-score 1.00
  • P36551 · AlphaFold monomer V2.0 prediction for oxygen-dependent coproporphyrinogen-III oxidase… · a predicted model of the same protein · chain A against A, TM-score 0.96

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