5eig

X-ray diffraction
2.7Å resolution

Engineered human cystathionine gamma lyase (E59T, E339V) to deplet cysteine

Released:
Source organism: Homo sapiens
Entry authors: Yan W, Zhang J

Function and Biology Details

Reactions catalysed:
(1a) L-cystathionine = L-cysteine + 2-aminobut-2-enoate
(1a) L-homocysteine = hydrogen sulfide + 2-aminobut-2-enoate

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-152515 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cystathionine gamma-lyase Chains: A, C, D, E, F, G
Molecule details ›
Chains: A, C, D, E, F, G
Length: 405 amino acids
Theoretical weight: 44.85 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:
Cystathionine gamma-lyase Chains: B, H
Molecule details ›
Chains: B, H
Length: 405 amino acids
Theoretical weight: 44.73 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

2 bound ligands:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Unit cell:
a: 113.377Å b: 163.455Å c: 181.625Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.233
Expression system: Escherichia coli