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Crystal structure of acyl CoA dehydrogenase

Analyse Crystal structure of acyl CoA dehydrogenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Z1Q
Type: protein
Length: 1,095 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acyl-CoA dehydrogenase
EC: 1.3.99.3
UniProt: Q5SJW0
Ligands: FAD
Pockets: 12 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 62% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acyl-CoA dehydrogenase (EC 1.3.99.3)	protein	546	62% helix, 11% strand	Q5SJW0
B	Acyl-CoA dehydrogenase (EC 1.3.99.3)	protein	549	62% helix, 10% strand	Q5SJW0

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	954	0.87	0.89	97	FAD
2	1103	0.86	0.87	137	FAD
3	1071	0.83	0.84	88	empty
4	213	0.70	0.87	36	empty
5	268	0.63	0.81	32	empty

Interfaces

1 interface between chains.

A–B · 3406 Å² buried · 63 hydrogen bonds · protein-protein

Compared structures

2Z1Q · Crystal structure of acyl CoA dehydrogenase · the same entry in another collection · 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 Q5SJW0
Elsewhere: RCSB PDB 2Z1Q · PDBe 2Z1Q · UniProt Q5SJW0

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