› 7pt3

X-ray diffraction
1.62Å resolution

Actinobacterial 2-hydroxyacyl-CoA lyase (AcHACL) mutant E493A structure in complex with substrate 2-HIB-CoA and inactive cofactor 3-deaza-ThDP

Released:
DOI: 10.2210/pdb7pt3/pdb
PDB entry 7pt3 coloured by chain, front view.
PDB entry 7pt3 coloured by chain, side view.
PDB entry 7pt3 coloured by chain, top view.
Source organism: Actinomycetospora chiangmaiensis DSM 45062
Primary publication:
Mechanistic details of the actinobacterial lyase-catalyzed degradation reaction of 2-hydroxyisobutyryl-CoA.
Zahn M, König G, Pham HVC, Seroka B, Lazny R, Yang G, Ouerfelli O, Lotowski Z, Rohwerder T
J Biol Chem 298 101522 (2022)
PMID: 34952003

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145137 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-hydroxyacyl-CoA lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 612 amino acids
Theoretical weight: 65.3 KDa
Source organism: Actinomycetospora chiangmaiensis DSM 45062
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0DUV9 (Residues: 1-590; Coverage: 100%)
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand TPW 2 x TPW
Ligand 3KK 2 x 3KK
Ligand MG 3 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2221
Unit cell:
a: 103.915Å b: 146.718Å c: 174.413Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.154 0.186
Expression system: Escherichia coli BL21(DE3)

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Citations

1 mention without citation

Mechanistic details of the actinobacterial lyase-catalyzed degradation reaction of 2-hydroxyisobutyryl-CoA.
Zahn et al. (2022)