Research workbench
F337R variant of human ferrochelatase
Analyse F337R variant of human ferrochelatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F4D
- 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
- CHD, FES, CL
- Pockets
- 11 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ferrochelatase, mitochondrial (EC 4.99.1.1) | protein | 359 | 50% helix, 14% strand | P22830 |
Ligands and binding sites
- CHD · Cholic acid · ligand · 6 copies · chains A, B
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 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 | 733 | 0.79 | 0.83 | 72 | FES, CHD |
| 2 | 117 | 0.78 | 0.97 | 36 | GOL |
| 3 | 699 | 0.77 | 0.82 | 50 | CL, CHD |
| 4 | 106 | 0.63 | 0.88 | 29 | FES |
| 5 | 272 | 0.61 | 0.79 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 1952 Ų buried · 36 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 4F4D · PDBe 4F4D · UniProt P22830
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