5vxo

X-ray diffraction
2.27Å resolution

Crystal Structure Analysis of human CLYBL in complex with propionyl-CoA

Released:
Source organism: Homo sapiens

Function and Biology Details

Reactions catalysed:
Acetyl-CoA + H(2)O + glyoxylate = (S)-malate + CoA
(S)-malyl-CoA + H(2)O = (S)-malate + CoA
(3S)-citramalyl-CoA = acetyl-CoA + pyruvate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-185345 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Citramalyl-CoA lyase, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 325 amino acids
Theoretical weight: 36.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8N0X4 (Residues: 30-340; Coverage: 92%)
Gene names: CLB, CLYBL
Sequence domains: HpcH/HpaI aldolase/citrate lyase family

Ligands and Environments


Cofactor: Ligand 1VU 3 x 1VU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 49.589Å b: 131.841Å c: 82.44Å
α: 90° β: 93.05° γ: 90°
R-values:
R R work R free
0.177 0.174 0.231
Expression system: Escherichia coli BL21(DE3)