Research workbench
Fech - inhibitor complex 1
Analyse Fech - inhibitor complex 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CTC
- 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
- FES, GFO
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Ferrochelatase, mitochondrial (EC 4.99.1.1) | protein | 359 | 52% helix, 14% strand | P22830 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, D
- GFO · 2-(4-tert-butylphenyl)-5-[(quinolin-2-ylamino)methyl]-6H-[1,2,4]triazolo[1,5-a]pyrimidin-7-one · ligand · 2 copies · chains A, D
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 | 140 | 0.79 | 0.97 | 38 | empty |
| 2 | 697 | 0.79 | 0.83 | 86 | FES, GFO |
| 3 | 536 | 0.77 | 0.84 | 59 | GFO |
| 4 | 119 | 0.60 | 0.86 | 31 | FES |
| 5 | 220 | 0.55 | 0.78 | 24 | empty |
Interfaces
1 interface between chains.
- A–D · 1920 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 7CTC · PDBe 7CTC · UniProt P22830
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