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Crystal structure of H183C bacillus subtilis ferrochelatase in complex with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride

Analyse Crystal structure of H183C bacillus subtilis ferrochelatase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Q2O
Type
protein
Length
307 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferrochelatase
EC
4.99.1.1
UniProt
P32396
Ligands
H01, MG
Pockets
1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFerrochelatase (EC 4.99.1.1)protein30750% helix, 17% strandP32396

Ligands and binding sites

  • H01 · Protoporphyrin IX 2,4-disulfonic acid · ligand · chains A
  • MG · Magnesium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15080.750.8362MG, H01

Compared structures

  • 2Q2O · Crystal structure of H183C Bacillus subtilis ferrochelatase in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • P32396 · AlphaFold monomer V2.0 prediction for coproporphyrin III ferrochelatase (P32396) · a predicted model of the same protein · chain A against A, TM-score 0.99

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