Research workbench
Crystal structure of human ferrochelatase mutant with his 341 replaced by cys
Analyse Crystal structure of human ferrochelatase mutant with his 341 replaced by cys in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PO7
- 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
- Pockets
- 10 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ferrochelatase, mitochondrial (EC 4.99.1.1) | protein | 359 | 51% 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
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.80 | 0.98 | 34 | empty |
| 2 | 730 | 0.78 | 0.82 | 72 | FES, CHD |
| 3 | 573 | 0.75 | 0.82 | 56 | CHD |
| 4 | 103 | 0.63 | 0.88 | 30 | FES |
| 5 | 225 | 0.54 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1833 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 2PO7 · Crystal structure of human ferrochelatase mutant with His 341 replaced by Cys · 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 2PO7 · PDBe 2PO7 · UniProt P22830
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