Research workbench
Structure of ferrochelatase with COPPER(II) N-methylmesoporphyrin complex bound at the active site
Analyse Structure of ferrochelatase with COPPER(II) N-methylmesoporphyrin complex bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protoheme ferrolyase (EC 4.99.1.1) | protein | 306 | 50% helix, 16% strand | P32396 |
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 652 | 0.76 | 0.81 | 59 | MG, 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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P32396
- Elsewhere: RCSB PDB 1C9E · PDBe 1C9E · UniProt P32396
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