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Crystal structure of human ferrochelatase
Analyse Crystal structure 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
- 1HRK
- 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
- Pockets
- 9 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ferrochelatase (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
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.78 | 0.98 | 32 | empty |
| 2 | 657 | 0.78 | 0.83 | 69 | CHD, FES |
| 3 | 565 | 0.74 | 0.81 | 53 | CHD |
| 4 | 96 | 0.59 | 0.87 | 27 | FES |
| 5 | 224 | 0.54 | 0.78 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1819 Ų buried · 34 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 1HRK · PDBe 1HRK · UniProt P22830
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