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Crystal structure of acyl-CoA dehydrogenase from mycobacterium thermoresistibile bound to flavin adenine dinucleotide

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

PDB: 3NF4
Type: protein
Length: 736 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acyl-CoA dehydrogenase
Ligands: FAD, NA
Pockets: 8 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acyl-CoA dehydrogenase	protein	369	53% helix, 15% strand	—
B	Acyl-CoA dehydrogenase	protein	367	54% helix, 16% strand	—

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A, B
NA · Sodium ion · metal · chains B

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

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	848	0.82	0.85	75	FAD
2	424	0.70	0.81	45	empty
3	308	0.62	0.79	28	empty
4	216	0.48	0.75	27	empty
5	79	0.47	0.82	24	empty

Interfaces

1 interface between chains.

A–B · 1711 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

3NF4 · Crystal structure of acyl-CoA dehydrogenase from Mycobacterium thermoresistibile bound to… · 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
Elsewhere: RCSB PDB 3NF4 · PDBe 3NF4

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