› 4myd

X-ray diffraction
1.37Å resolution

1.37 Angstrom Crystal Structure of E. Coli 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (MenH) in complex with SHCHC

Released:
DOI: 10.2210/pdb4myd/pdb
PDB entry 4myd coloured by chain, front view.
PDB entry 4myd coloured by chain, side view.
PDB entry 4myd coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Molecular basis of the general base catalysis of an α/β-hydrolase catalytic triad.
Sun Y, Yin S, Feng Y, Li J, Zhou J, Liu C, Zhu G, Guo Z
J Biol Chem 289 15867-79 (2014)
PMID: 24737327

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: 252 amino acids
Theoretical weight: 27.71 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
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

1 bound ligand:
Ligand 164 2 x 164
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P31
Unit cell:
a: 121.85Å b: 121.85Å c: 46.85Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.13 0.128 0.166
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Mechanisms of ligand binding.
Di Cera E. (2020)
10 other articles

3 mentions without citation

Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.
Houben et al. (2020)
2 more