Research workbench
H235C variant of yeast ferrochelatase
Analyse H235C variant of yeast ferrochelatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L78
- Type
- protein
- Length
- 711 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferrochelatase, mitochondrial
- EC
- 4.99.1.1
- UniProt
- P16622
- Ligands
- CHD
- Pockets
- 9 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferrochelatase, mitochondrial (EC 4.99.1.1) | protein | 356 | 49% helix, 14% strand | P16622 |
| B | Ferrochelatase, mitochondrial (EC 4.99.1.1) | protein | 355 | 50% helix, 14% strand | P16622 |
Ligands and binding sites
- CHD · Cholic acid · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.82 | 0.98 | 39 | empty |
| 2 | 809 | 0.79 | 0.82 | 60 | empty |
| 3 | 683 | 0.75 | 0.81 | 55 | CHD |
| 4 | 287 | 0.59 | 0.78 | 28 | empty |
| 5 | 277 | 0.54 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1519 Ų buried · 23 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 P16622
- Elsewhere: RCSB PDB 7L78 · PDBe 7L78 · UniProt P16622
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