MolNFT v1 · #34933 · protein

Crystal structure of project TT0160 from thermus thermophilus HB8

2DVL · Acyl-CoA dehydrogenase: “Crystal structure of project TT0160 from thermus thermophilus HB8”. X-ray diffraction, 1 ligand (FAD), 4 pockets (best druggability 0.77). MolNFT v1 #34933 on GenesisL1: 3D structure, binding sites and…

PDB: 2DVL
Type: protein
Length: 740 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acyl-CoA dehydrogenase
UniProt: Q5SH14
Ligands: FAD
Pockets: 4 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Acyl-CoA dehydrogenase	protein	370	59% helix, 16% strand	Q5SH14

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

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	586	0.77	0.83	70	FAD
2	653	0.76	0.82	71	FAD
3	537	0.62	0.74	59	empty
4	212	0.52	0.77	21	empty

Interfaces

1 interface between chains.

A–B · 1354 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2DVL · Crystal structure of project TT0160 from Thermus thermophilus HB8 · 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 Q5SH14
Elsewhere: RCSB PDB 2DVL · PDBe 2DVL · UniProt Q5SH14

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