› 2fq6

X-ray diffraction
1.78Å resolution

Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-trifluoromethyl-benzamide

Released:
DOI: 10.2210/pdb2fq6/pdb
PDB entry 2fq6 coloured by chain, front view.
PDB entry 2fq6 coloured by chain, side view.
PDB entry 2fq6 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Inhibitors of bacterial cystathionine beta-lyase: leads for new antimicrobial agents and probes of enzyme structure and function.
Ejim LJ, Blanchard JE, Koteva KP, Sumerfield R, Elowe NH, Chechetto JD, Brown ED, Junop MS, Wright GD
J Med Chem 50 755-64 (2007)
PMID: 17300162

Function and Biology Details

Reactions catalysed: 
(1a) an L-cysteine-S-conjugate = a thiol + 2-aminoporp-2-enoate
 (1a) L-cysteine = 2-aminoprop-2-enoate + sulfide
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-139159 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cystathionine beta-lyase MetC Chains: A, B
Molecule details ›
Chains: A, B
Length: 415 amino acids
Theoretical weight: 45.43 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06721 (Residues: 1-395; Coverage: 100%)
Gene names: JW2975, b3008, metC
Sequence domains: Cys/Met metabolism PLP-dependent enzyme
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand P3F 2 x P3F
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2221
Unit cell:
a: 59.83Å b: 153.47Å c: 151.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.169 0.225
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Drug targets in mycobacterial sulfur metabolism.
Bhave et al. (2007)
2 more

4 mentions without citation

Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.
Naz et al. (2023)
3 more