› 4l27

X-ray diffraction
3.39Å resolution

Crystal structure of delta1-39 and delta516-525 human cystathionine beta-synthase D444N mutant containing C-terminal 6xHis tag

Released:
DOI: 10.2210/pdb4l27/pdb
PDB entry 4l27 coloured by chain, front view.
PDB entry 4l27 coloured by chain, side view.
PDB entry 4l27 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of regulation and oligomerization of human cystathionine β-synthase, the central enzyme of transsulfuration.
Ereño-Orbea J, Majtan T, Oyenarte I, Kraus JP, Martínez-Cruz LA
Proc Natl Acad Sci U S A 110 E3790-9 (2013)
PMID: 24043838

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-152934 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cystathionine beta-synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 548 amino acids
Theoretical weight: 60.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35520 (Residues: 2-551; Coverage: 98%)
Gene name: CBS
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM

Cofactor: Ligand PLP 4 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P65
Unit cell:
a: 190.454Å b: 190.454Å c: 140.847Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.206 0.244
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

The therapeutic potential of cystathionine β-synthetase/hydrogen sulfide inhibition in cancer.
Hellmich et al. (2015)
17 more

3 mentions without citation

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