› 3lnp

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reactions catalysed: 
S-adenosyl-L-homocysteine + H(2)O = S-inosyl-L-homocysteine + NH(3)
S-methyl-5'-thioadenosine + H(2)O = S-methyl-5'-thioinosine + NH(3)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112518 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5-methylthioadenosine/S-adenosylhomocysteine deaminase Chain: A
Molecule details ›
Chain: A
Length: 468 amino acids
Theoretical weight: 51.6 KDa
Source organism: Oleispira antarctica
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: D3KFX9 (Residues: 1-468; Coverage: 100%)
Gene name: mtaD
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand ACY 2 x ACY
Ligand PEG 1 x PEG
1 modified residue:
Ligand MSE 13 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P3221
Unit cell:
a: 77.902Å b: 77.902Å c: 143.754Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.151 0.149 0.184
Expression system: Escherichia coli BL21

Quick links

Citations

13 review citations

Estimating the success of enzyme bioprospecting through metagenomics: current status and future trends.
Ferrer et al. (2016)
12 more

4 mentions without citation

Genome sequence and functional genomic analysis of the oil-degrading bacterium Oleispira antarctica.
Kube et al. (2013)
3 more