› 3mp5

X-ray diffraction
2.25Å resolution

Crystal Structure of Human Lyase R41M in complex with HMG-CoA

Released:
DOI: 10.2210/pdb3mp5/pdb
PDB entry 3mp5 coloured by chain, front view.
PDB entry 3mp5 coloured by chain, side view.
PDB entry 3mp5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Functional insights into human HMG-CoA lyase from structures of Acyl-CoA-containing ternary complexes.
Fu Z, Runquist JA, Montgomery C, Miziorko HM, Kim JJ
J Biol Chem 285 26341-9 (2010)
PMID: 20558737

Function and Biology Details

Reaction catalysed: 
(S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153052 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxymethylglutaryl-CoA lyase, mitochondrial Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 298 amino acids
Theoretical weight: 31.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35914 (Residues: 28-325; Coverage: 92%)
Gene name: HMGCL
Sequence domains: HMGL-like
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand HMG 1 x HMG
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2
Unit cell:
a: 197.98Å b: 116.66Å c: 86.52Å
α: 90° β: 112.16° γ: 90°
R-values:
R R work R free
0.221 0.221 0.271
Expression system: Escherichia coli

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Citations

1 review citation

Enzymes of the mevalonate pathway of isoprenoid biosynthesis.
Miziorko HM. (2011)
10 other articles

2 mentions without citation

An essential bifunctional enzyme in Mycobacterium tuberculosis for itaconate dissimilation and leucine catabolism.
Wang et al. (2019)
1 more