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Crystal structure of B. subtilis ferrochelatase with cobalt bound at the active site

Analyse Crystal structure of B. subtilis ferrochelatase with cobalt bound at the active… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3M4Z
Type
protein
Length
309 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
MG, CO, CL
Pockets
1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFerrochelatase (EC 4.99.1.1)protein30949% helix, 17% strandP32396

Ligands and binding sites

  • MG · Magnesium ion · metal · 3 copies · chains A
  • CO · Cobalt (II) ion · metal · chains A
  • CL · Chloride ion · ion · 2 copies · 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
15200.770.8461CO, MG

Compared structures

  • 3M4Z · Crystal Structure of B. subtilis ferrochelatase with Cobalt bound at the active site · 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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