› 5m3z

X-ray diffraction
1.45Å resolution

Crystal structure of Citrobacter freundii methionine gamma-lyase with C115H replacement in the complex with L-norleucine

Released:
DOI: 10.2210/pdb5m3z/pdb
PDB entry 5m3z coloured by chain, front view.
PDB entry 5m3z coloured by chain, side view.
PDB entry 5m3z coloured by chain, top view.
Source organism: Citrobacter freundii
Primary publication:
Crystal structure of mutant form Cys115His of Citrobacter freundii methionine γ-lyase complexed with l-norleucine.
Revtovich SV, Morozova EA, Kulikova VV, Anufrieva NV, Osipova TI, Koval VS, Nikulin AD, Demidkina TV
Biochim Biophys Acta Proteins Proteom 1865 1123-1128 (2017)
PMID: 28602917

Function and Biology Details

Reaction catalysed: 
(1a) L-methionine = methanethiol + 2-aminobut-2-enoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100816 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-methionine gamma-lyase Chain: A
Molecule details ›
Chain: A
Length: 398 amino acids
Theoretical weight: 42.99 KDa
Source organism: Citrobacter freundii
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: A0A0A5P8W7 (Residues: 1-398; Coverage: 100%)
Gene names: AI2602V1_0214, AI2935V1_0207, AN672_11005, HV333_01080, HXS83_00935, I9Y29_001146, JDY53_20795, KV121_003196, KY227_003757, TO64_18625, megL
Sequence domains: Cys/Met metabolism PLP-dependent enzyme

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
3 bound ligands:
Ligand NLE 1 x NLE
Ligand PGE 1 x PGE
Ligand PY6 1 x PY6
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: I222
Unit cell:
a: 56.513Å b: 123.019Å c: 127.577Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.13 0.128 0.169
Expression system: Escherichia coli K-12

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Citations

2 citation in other articles

New N-Alkylated Heterocyclic Compounds as Prospective NDM1 Inhibitors: Investigation of In Vitro and In Silico Properties.
Kaddouri et al. (2022)
1 more