Research workbench

BD2924 C10 acyl-coenzymea bound form

Analyse BD2924 C10 acyl-coenzymea bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SDA
Type: protein
Length: 1,006 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable acyl-CoA dehydrogenase
EC: 1.3.99.-
UniProt: Q6MJ59
Ligands: FAD, MFK
Pockets: 6 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Probable acyl-CoA dehydrogenase (EC 1.3.99.-)	protein	503	57% helix, 14% strand	Q6MJ59

Ligands and binding sites

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

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

Pockets

6 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	1033	0.85	0.85	125	FAD
2	1067	0.84	0.84	113	MFK, FAD
3	420	0.61	0.76	37	empty
4	114	0.48	0.80	18	empty
5	138	0.42	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 2571 Å² buried · 41 hydrogen bonds · protein-protein

Compared structures

6SDA · Bd2924 C10 acyl-coenzymeA bound form · 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 Q6MJ59
Elsewhere: RCSB PDB 6SDA · PDBe 6SDA · UniProt Q6MJ59

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