› 4l0d

X-ray diffraction
2.97Å resolution

Crystal structure of delta516-525 human cystathionine beta-synthase containing C-terminal 6xHis-tag

Released:
DOI: 10.2210/pdb4l0d/pdb
PDB entry 4l0d coloured by chain, front view.
PDB entry 4l0d coloured by chain, side view.
PDB entry 4l0d 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
Molecule details ›
Chains: A, B
Length: 549 amino acids
Theoretical weight: 60.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35520 (Residues: 1-551; Coverage: 98%)
Gene name: CBS
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP

Cofactor: Ligand HEM 2 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: I222
Unit cell:
a: 124.365Å b: 136.203Å c: 169.307Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.24 0.284
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

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

7 mentions without citation

Structural Basis for Allostery in PLP-dependent Enzymes.
Tran et al. (2022)
6 more