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MolNFT v1 · #2858 · protein

Structure of ferrochelatase with COPPER(II) N-methylmesoporphyrin complex bound at the active site

1C9E · Protoheme ferrolyase: “Structure of ferrochelatase with COPPER(II) N-methylmesoporphyrin complex bound at the active site”. X-ray diffraction, 2 ligands (MP1, MG), 1 pocket (best druggability 0.76). MolNFT v1 #2858 on GenesisL1: 3D…

PDB
1C9E
Type
protein
Length
306 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protoheme ferrolyase
EC
4.99.1.1
UniProt
P32396
Ligands
MP1, MG
Pockets
1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtoheme ferrolyase (EC 4.99.1.1)protein30650% helix, 16% strandP32396

Ligands and binding sites

  • MP1 · N-methylmesoporphyrin containing copper · 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
16520.760.8159MG, MP1

Compared structures

  • 1C9E · Structure of ferrochelatase with COPPER(II) N-methylmesoporphyrin complex bound at the… · 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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