› 3elp

X-ray diffraction
2.4Å resolution

Function and Biology Details

Reactions catalysed: 
(1a) L-cystathionine = L-cysteine + 2-aminobut-2-enoate
(1a) L-homocysteine = hydrogen sulfide + 2-aminobut-2-enoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152516 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cystathionine gamma-lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 410 amino acids
Theoretical weight: 45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P32929 (Residues: 1-405; Coverage: 100%)
Gene name: CTH
Sequence domains: Cys/Met metabolism PLP-dependent enzyme
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P42
Unit cell:
a: 121.304Å b: 121.304Å c: 125.592Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.222 0.236
Expression system: Escherichia coli

Quick links

Citations

33 review citations

Chemical Biology of H2S Signaling through Persulfidation.
Filipovic et al. (2018)
32 more

7 mentions without citation

Cystathionine gamma-lyase: Clinical, metabolic, genetic, and structural studies.
Kraus et al. (2009)
6 more