› 3pc3

X-ray diffraction
1.55Å resolution

Full length structure of cystathionine beta-synthase from Drosophila in complex with aminoacrylate

Released:
DOI: 10.2210/pdb3pc3/pdb
PDB entry 3pc3 coloured by chain, front view.
PDB entry 3pc3 coloured by chain, side view.
PDB entry 3pc3 coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine {beta}-synthase.
Koutmos M, Kabil O, Smith JL, Banerjee R
Proc Natl Acad Sci U S A 107 20958-63 (2010)
PMID: 21081698

Function and Biology Details

Reaction catalysed: 
L-serine + L-homocysteine = L-cystathionine + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-194294 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cystathionine beta-synthase Chain: A
Molecule details ›
Chain: A
Length: 527 amino acids
Theoretical weight: 57.47 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9VRD9 (Residues: 1-522; Coverage: 100%)
Gene names: CBS, CG1753, Cbs, DmCBS, Dmel\CG1753, Dmel_CG1753, dCBS
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
Ligand P1T 1 x P1T
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2221
Unit cell:
a: 93.275Å b: 138.815Å c: 75.146Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.148 0.188
Expression system: Escherichia coli BL21

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Citations

12 review citations

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

10 mentions without citation

PLP-dependent H(2)S biogenesis.
Singh et al. (2011)
9 more