› 5ugr

X-ray diffraction
1.56Å resolution

Malyl-CoA lyase from Methylobacterium extorquens

Released:
DOI: 10.2210/pdb5ugr/pdb
PDB entry 5ugr coloured by chain, front view.
PDB entry 5ugr coloured by chain, side view.
PDB entry 5ugr coloured by chain, top view.
Source organism: Methylorubrum extorquens AM1
Primary publication:
Structure of Methylobacterium extorquens malyl-CoA lyase: CoA-substrate binding correlates with domain shift.
Gonz��lez JM, Marti-Arbona R, Chen JC, Unkefer CJ
Acta Crystallogr F Struct Biol Commun 73 79-85 (2017)
PMID: 28177317

Function and Biology Details

Reaction catalysed: 
(2R,3S)-2-methylmalyl-CoA = propanoyl-CoA + glyoxylate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111458 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HpcH/HpaI aldolase/citrate lyase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 333 amino acids
Theoretical weight: 36.73 KDa
Source organism: Methylorubrum extorquens AM1
Expression system: Escherichia coli
UniProt:
  • Canonical: C5B113 (Residues: 1-324; Coverage: 100%)
Gene names: MexAM1_META1p1733, mcl
Sequence domains: HpcH/HpaI aldolase/citrate lyase family
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand CL 1 x CL
Ligand 1PE 1 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P622
Unit cell:
a: 126.524Å b: 126.524Å c: 103.207Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.104 0.102 0.134
Expression system: Escherichia coli

Quick links

Citations

2 mentions without citation

Thioesterase enzyme families: Functions, structures, and mechanisms.
Caswell et al. (2022)
1 more