› 4gdm

X-ray diffraction
2.75Å resolution

Crystal Structure of E.coli MenH

Released:
DOI: 10.2210/pdb4gdm/pdb
PDB entry 4gdm coloured by chain, front view.
PDB entry 4gdm coloured by chain, side view.
PDB entry 4gdm coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Crystal structures of E. coli native MenH and two active site mutants.
Johnston JM, Jiang M, Guo Z, Baker EN
PLoS One 8 e61325 (2013)
PMID: 23637813

Function and Biology Details

Reaction catalysed: 
5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate + pyruvate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153402 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 268 amino acids
Theoretical weight: 29.52 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P37355 (Residues: 1-252; Coverage: 100%)
Gene names: JW2258, b2263, menH, yfbB
Sequence domains: Alpha/beta hydrolase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand SO4 4 x SO4
Ligand CL 3 x CL
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: I4122
Unit cell:
a: 116.664Å b: 116.664Å c: 476.949Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.192 0.223
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Biosynthesis and applications of prenylquinones.
Kawamukai M. (2018)
2 other articles

2 mentions without citation

Molecular basis of the general base catalysis of an α/β-hydrolase catalytic triad.
Sun et al. (2014)
1 more