› 5tt2

X-ray diffraction
2.95Å resolution

Inactive conformation of engineered human cystathionine gamma lyase (E59N, R119L, E339V) to depleting methionine

Released:
DOI: 10.2210/pdb5tt2/pdb
PDB entry 5tt2 coloured by chain, front view.
PDB entry 5tt2 coloured by chain, side view.
PDB entry 5tt2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Snapshots of an Engineered Cystathionine-γ-lyase Reveal the Critical Role of Electrostatic Interactions in the Active Site.
Yan W, Stone E, Zhang YJ
Biochemistry 56 876-885 (2017)
PMID: 28106980

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: C, D
Molecule details ›
Chains: C, D
Length: 422 amino acids
Theoretical weight: 46.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P32929 (Residues: 2-405; Coverage: 100%)
Gene name: CTH
Sequence domains: Cys/Met metabolism PLP-dependent enzyme

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P42212
Unit cell:
a: 120.224Å b: 120.224Å c: 125.622Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.2 0.254
Expression system: Escherichia coli BL21

Quick links

Citations

5 citation in other articles

Snapshots of C-S Cleavage in Egt2 Reveals Substrate Specificity and Reaction Mechanism.
Irani et al. (2018)
4 more

1 mention without citation

Structural Snapshots of an Engineered Cystathionine-γ-lyase Reveal the Critical Role of Electrostatic Interactions in the Active Site.
Yan et al. (2017)