MolNFT v1 · #93814 · protein

Crystal structure of a carnitinyl-CoA dehydratase from mycobacterium thermoresistibile

4HDT · 3-hydroxyisobutyryl-CoA hydrolase: “Crystal structure of a carnitinyl-CoA dehydratase from mycobacterium thermoresistibile”. X-ray diffraction, 2 ligands (ZN, CL), 5 pockets (best druggability 0.62). MolNFT v1 #93814 on GenesisL1…

PDB: 4HDT
Type: protein
Length: 340 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-hydroxyisobutyryl-CoA hydrolase
UniProt: G7CC99
Ligands: ZN, CL
Pockets: 5 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-hydroxyisobutyryl-CoA hydrolase	protein	340	54% helix, 12% strand	G7CC99

Ligands and binding sites

ZN · Zinc ion · metal · 5 copies · chains A
CL · Chloride ion · ion · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	185	0.62	0.83	28	empty
2	87	0.40	0.78	15	empty
3	91	0.40	0.77	24	empty
4	77	0.36	0.76	14	empty
5	54	0.30	0.75	17	empty

Compared structures

4HDT · Crystal structure of a Carnitinyl-CoA dehydratase from Mycobacterium thermoresistibile · 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 G7CC99
Elsewhere: RCSB PDB 4HDT · PDBe 4HDT · UniProt G7CC99

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.