› 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 7pt3 coloured by chain and viewed from the front.
PDB 7pt3 coloured by chain and viewed from the side.
PDB 7pt3 coloured by chain and viewed from the top.
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:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (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%)

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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