Crystal structure of human acyl-CoA synthetase medium-chain family member 2A (L64P mutation) in complex with AMP

Structural Snapshots for the Conformation- Dependent Catalysis by Human Medium-Chain Acyl- Coenzyme a Synthetase Acsm2A.

ACYL-COENZYME A SYNTHETASE ACSM2A, MITOCHONDRIAL

ACYL-COA SYNTHETASE MEDIUM-CHAIN FAMILY MEMBER 2A, MIDDLE-CHAIN ACYL-COA SYNTHETASE 2A, BUTYRYL COENZYME A SYNTHETASE 2A, BUTYRATE--COA LIGASE 2A

0.2M AMMONIUM ACETATE, 0.1M TRIS PH 8.5, 25% PEG 3350

SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.

ENGINEERED RESIDUE IN CHAIN A, LEU 64 TO PRO ENGINEERED RESIDUE IN CHAIN B, LEU 64 TO PRO ENGINEERED RESIDUE IN CHAIN C, LEU 64 TO PRO

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

ACYL-COENZYME A SYNTHETASE ACSM2A, MITOCHONDRIAL (E.C.6.2.1.2)

LIGASE, METAL-BINDING, TRANSIT PEPTIDE, LIPID METABOLISM, NUCLEOTIDE-BINDING, ATP-BINDING, ADENYLATE-FORMING ENZYME, FATTY ACID METABOLISM, FATTY ACID-COA LIGASE