› 4itg

X-ray diffraction
1.74Å resolution

P113S mutant of E. coli Cystathionine beta-lyase MetC

Released:
DOI: 10.2210/pdb4itg/pdb
PDB entry 4itg coloured by chain, front view.
PDB entry 4itg coloured by chain, side view.
PDB entry 4itg coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Mechanistic and Evolutionary Insights from the Reciprocal Promiscuity of Two Pyridoxal Phosphate-dependent Enzymes.
Soo VW, Yosaatmadja Y, Squire CJ, Patrick WM
OpenAccess logo J Biol Chem 291 19873-87 (2016)
PMID: 27474741

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 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: 395 amino acids
Theoretical weight: 43.48 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
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 EPE 2 x EPE
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2221
Unit cell:
a: 59.926Å b: 152.769Å c: 150.848Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.198
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Review: Engineering of thermostable enzymes for industrial applications.
Rigoldi et al. (2018)
3 more

3 mentions without citation

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