MolNFT v1 · #49837 · protein
The effect of a GLU370ASP mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate
2R0N: “The effect of a GLU370ASP mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate…”. X-ray diffraction, 2 ligands (FAD, TGC), 3 pockets (best druggability 0.72). MolNFT v1 #49837 on GenesisL1: 3D structure…
- PDB
- 2R0N
- Type
- protein
- Length
- 390 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaryl-CoA dehydrogenase
- EC
- 1.3.99.7
- UniProt
- Q92947
- Ligands
- FAD, TGC
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutaryl-CoA dehydrogenase (EC 1.3.99.7) | protein | 390 | 55% helix, 15% strand | Q92947 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 399 | 0.72 | 0.82 | 42 | FAD, TGC |
| 2 | 148 | 0.48 | 0.78 | 26 | empty |
| 3 | 107 | 0.47 | 0.80 | 23 | empty |
Compared structures
- 2R0N · The effect of a Glu370Asp mutation in Glutaryl-CoA Dehydrogenase on Proton Transfer to… · the same entry in another collection · chain A against A, TM-score 1.00
- Q92947 · AlphaFold monomer V2.0 prediction for glutaryl-CoA dehydrogenase, mitochondrial (Q92947) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q92947
- Elsewhere: RCSB PDB 2R0N · PDBe 2R0N · UniProt Q92947
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