› 1cs1

X-ray diffraction
1.5Å resolution

CYSTATHIONINE GAMMA-SYNTHASE (CGS) FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1cs1/pdb
PDB entry 1cs1 coloured by chain, front view.
PDB entry 1cs1 coloured by chain, side view.
PDB entry 1cs1 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution.
Clausen T, Huber R, Prade L, Wahl MC, Messerschmidt A
EMBO J 17 6827-38 (1998)
PMID: 9843488

Function and Biology Details

Reaction catalysed: 
O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133698 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cystathionine gamma-synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 386 amino acids
Theoretical weight: 41.83 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00935 (Residues: 1-386; Coverage: 100%)
Gene names: JW3910, b3939, metB
Sequence domains: Cys/Met metabolism PLP-dependent enzyme
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand DHD 1 x DHD
1 modified residue:
Ligand LLP 4 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: C2
Unit cell:
a: 160.04Å b: 61.3Å c: 153.84Å
α: 90° β: 104.18° γ: 90°
R-values:
R R work R free
0.2 0.2 0.255
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

The manifold of vitamin B6 dependent enzymes.
Schneider et al. (2000)
3 more

8 mentions without citation

Macro-to-micro structural proteomics: native source proteins for high-throughput crystallization.
Totir et al. (2012)
7 more