5tsu

X-ray diffraction
2.2Å resolution

Active conformation for Engineered human cystathionine gamma lyase (E59N, R119L, E339V) to depleting methionine

Released:

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, B, D, F, G, H
Molecule details ›
Chains: A, B, D, F, G, H
Length: 422 amino acids
Theoretical weight: 46.58 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
Cystathionine gamma-lyase Chains: C, E
Molecule details ›
Chains: C, E
Length: 422 amino acids
Theoretical weight: 46.36 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 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Unit cell:
a: 111.889Å b: 163.683Å c: 181.099Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.171 0.202
Expression system: Escherichia coli BL21