Research workbench
1.7 ångström structure of human ferrochelatase variant R115L
Analyse 1.7 ångström structure of human ferrochelatase variant R115L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HRC
- Type
- protein
- Length
- 718 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferrochelatase
- EC
- 4.99.1.1
- UniProt
- P22830
- Ligands
- CHD, FES, CL
- Pockets
- 11 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ferrochelatase (EC 4.99.1.1) | protein | 359 | 49% 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
- IMD · Imidazole · additive · 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 | 107 | 0.79 | 0.98 | 30 | GOL |
| 2 | 746 | 0.78 | 0.82 | 81 | CL, FES, IMD, CHD |
| 3 | 608 | 0.75 | 0.82 | 48 | CL, IMD, CHD |
| 4 | 83 | 0.65 | 0.91 | 28 | FES |
| 5 | 288 | 0.61 | 0.79 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1868 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 2HRC · 1.7 angstrom structure of human ferrochelatase variant R115L · the same entry in another collection · chain A against A, TM-score 1.00
- P22830 · AlphaFold monomer V2.0 prediction for ferrochelatase, mitochondrial (P22830) · 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 P22830
- Elsewhere: RCSB PDB 2HRC · PDBe 2HRC · UniProt P22830
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