MolNFT v1 · #97651 · protein
E343D/F110A double mutant of human ferrochelatase
4KLC · Ferrochelatase, mitochondrial: “E343D/F110A double mutant of human ferrochelatase”. X-ray diffraction, 2 ligands (FES, HEM), 11 pockets (best druggability 0.80). MolNFT v1 #97651 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4KLC
- Type
- protein
- Length
- 718 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferrochelatase, mitochondrial
- EC
- 4.99.1.1
- UniProt
- P22830
- Ligands
- FES, HEM
- Pockets
- 11 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ferrochelatase, mitochondrial (EC 4.99.1.1) | protein | 359 | 48% helix, 14% strand | P22830 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, B
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 669 | 0.80 | 0.84 | 79 | FES, HEM |
| 2 | 128 | 0.79 | 0.97 | 33 | GOL |
| 3 | 684 | 0.78 | 0.83 | 69 | FES, HEM |
| 4 | 50 | 0.67 | 0.97 | 19 | FES |
| 5 | 245 | 0.58 | 0.79 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1838 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
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 P22830
- Elsewhere: RCSB PDB 4KLC · PDBe 4KLC · UniProt P22830
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