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X-ray structure of acyl-CoA thioesterase I, tesa, mutant M141L/Y145K/L146K at pH 7.5 in complex with octanoic acid

Analyse X-ray structure of acyl-CoA thioesterase I, tesa, mutant M141L/Y145K/L146K at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TIE
Type: protein
Length: 181 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acyl-CoA thioesterase I
EC: 3.1.2.-, 3.1.1.5
UniProt: P0ADA1
Ligands: OCA
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acyl-CoA thioesterase I (EC 3.1.2.-, 3.1.1.5)	protein	181	53% helix, 15% strand	P0ADA1

Ligands and binding sites

OCA · Octanoic acid (caprylic acid) · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.56	0.86	20	OCA

Compared structures

P0ADA1 · AlphaFold monomer V2.0 prediction for thioesterase 1/PROTEASE 1/LYSOPHOSPHOLIPASE L1… · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P0ADA1
Elsewhere: RCSB PDB 5TIE · PDBe 5TIE · UniProt P0ADA1

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