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Structural study on project id TT0172 from thermus thermophilus HB8

Analyse Structural study on project id TT0172 from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2D29
Type: protein
Length: 772 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acyl-CoA dehydrogenase
UniProt: Q5SGZ2
Ligands: FAD
Pockets: 9 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Acyl-CoA dehydrogenase	protein	386	58% helix, 15% strand	Q5SGZ2

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

9 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	491	0.72	0.81	54	FAD
2	507	0.72	0.81	54	FAD
3	366	0.59	0.76	31	empty
4	148	0.56	0.81	28	empty
5	138	0.54	0.81	24	empty

Interfaces

1 interface between chains.

A–B · 1919 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2D29 · Structural study on project ID TT0172 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 Q5SGZ2
Elsewhere: RCSB PDB 2D29 · PDBe 2D29 · UniProt Q5SGZ2

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