› 2e7z

X-ray diffraction
1.26Å resolution

Acetylene Hydratase from Pelobacter acetylenicus

Released:
DOI: 10.2210/pdb2e7z/pdb
PDB entry 2e7z coloured by chain, front view.
PDB entry 2e7z coloured by chain, side view.
PDB entry 2e7z coloured by chain, top view.
Source organism: Syntrophotalea acetylenica
Primary publication:
Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase.
Seiffert GB, Ullmann GM, Messerschmidt A, Schink B, Kroneck PM, Einsle O
Proc Natl Acad Sci U S A 104 3073-7 (2007)
PMID: 17360611

Function and Biology Details

Reaction catalysed: 
Acetaldehyde = acetylene + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180747 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylene hydratase Chain: A
Molecule details ›
Chain: A
Length: 727 amino acids
Theoretical weight: 81.65 KDa
Source organism: Syntrophotalea acetylenica
UniProt:
  • Canonical: Q71EW5 (Residues: 4-730; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand MGD 2 x MGD
5 bound ligands:
Ligand NA 1 x NA
Ligand ACT 1 x ACT
Ligand SF4 1 x SF4
Ligand W 1 x W
Ligand MPD 2 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6, EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 120.776Å b: 71.971Å c: 106.76Å
α: 90° β: 124.26° γ: 90°
R-values:
R R work R free
0.161 0.16 0.195

Quick links

Citations

13 review citations

Chemical analogues relevant to molybdenum and tungsten enzyme reaction centres toward structural dynamics and reaction diversity.
Sugimoto et al. (2008)
12 more

8 mentions without citation

On the current role of hydratases in biocatalysis.
Engleder et al. (2018)
7 more