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The crystal structure and mechanism of human glutaryl-CoA dehydrogenase

Analyse The crystal structure and mechanism of human glutaryl-CoA dehydrogenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SIQ
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
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutaryl-CoA dehydrogenase (EC 1.3.99.7)	protein	390	56% helix, 16% strand	Q92947

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	443	0.72	0.82	46	FAD
2	116	0.37	0.74	21	empty
3	52	0.29	0.76	12	empty

Compared structures

1SIQ · The Crystal Structure and Mechanism of Human Glutaryl-CoA Dehydrogenase · 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 1SIQ · PDBe 1SIQ · UniProt Q92947

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