› 2e7z

X-ray diffraction
1.26Å resolution

Acetylene Hydratase from Pelobacter acetylenicus

Released:
DOI: 10.2210/pdb2e7z/pdb
Model geometry
Fit model/data
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

wwPDB Validation report is not available for this entry.
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

14 review citations

The prokaryotic Mo/W-bisPGD enzymes family: a catalytic workhorse in bioenergetic.
Grimaldi et al. (2013)
13 more

8 mentions without citation

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