› 3pc4

X-ray diffraction
1.7Å resolution

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

Released:
DOI: 10.2210/pdb3pc4/pdb
PDB entry 3pc4 coloured by chain, front view.
PDB entry 3pc4 coloured by chain, side view.
PDB entry 3pc4 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

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194295 (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
2 bound ligands:
Ligand KOU 1 x KOU
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2221
Unit cell:
a: 92.947Å b: 137.935Å c: 75.129Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.203
Expression system: Escherichia coli BL21

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Citations

11 review citations

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

12 mentions without citation

Enzymology of H2S biogenesis, decay and signaling.
Kabil et al. (2014)
11 more