Magnesium in PDB 1sww: Crystal Structure of the Phosphonoacetaldehyde Hydrolase D12A Mutant Complexed with Magnesium and Substrate Phosphonoacetaldehyde

All present enzymatic activity of Crystal Structure of the Phosphonoacetaldehyde Hydrolase D12A Mutant Complexed with Magnesium and Substrate Phosphonoacetaldehyde:
3.11.1.1;

The structure of Crystal Structure of the Phosphonoacetaldehyde Hydrolase D12A Mutant Complexed with Magnesium and Substrate Phosphonoacetaldehyde, PDB code: 1sww was solved by G.Zhang, M.C.Morais, J.Dai, W.Zhang, D.Dunaway-Mariano, K.N.Allen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.68 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.815, 62.520, 72.618, 90.00, 108.03, 90.00
R / Rfree (%)	21.8 / 27.8

The binding sites of Magnesium atom in the Crystal Structure of the Phosphonoacetaldehyde Hydrolase D12A Mutant Complexed with Magnesium and Substrate Phosphonoacetaldehyde (pdb code 1sww). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Phosphonoacetaldehyde Hydrolase D12A Mutant Complexed with Magnesium and Substrate Phosphonoacetaldehyde, PDB code: 1sww:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Phosphonoacetaldehyde Hydrolase D12A Mutant Complexed with Magnesium and Substrate Phosphonoacetaldehyde


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Phosphonoacetaldehyde Hydrolase D12A Mutant Complexed with Magnesium and Substrate Phosphonoacetaldehyde within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:20.0 occ:1.00 O1P A:POA600 2.3 50.4 1.0 OD1 A:ASP186 2.6 16.9 1.0 OD2 A:ASP190 2.6 11.1 1.0 O A:HOH656 2.9 15.6 1.0 O A:ALA14 3.1 10.1 1.0 CB A:ALA12 3.2 12.2 1.0 O2P A:POA600 3.3 53.5 1.0 O A:HOH694 3.4 16.9 1.0 P A:POA600 3.4 52.5 1.0 CG A:ASP190 3.5 10.1 1.0 CG A:ASP186 3.6 17.9 1.0 OD1 A:ASP190 3.7 8.9 1.0 CG2 A:THR187 3.9 9.5 1.0 OD2 A:ASP186 4.0 17.5 1.0 NH1 A:ARG160 4.1 16.4 1.0 OG1 A:THR16 4.2 13.7 1.0 C A:ALA14 4.3 9.5 1.0 NH2 A:ARG160 4.3 11.2 1.0 N A:ASP186 4.4 15.2 1.0 CZ A:ARG160 4.4 13.6 1.0 N A:TRP13 4.4 11.5 1.0 OG1 A:THR187 4.5 12.4 1.0 CA A:ALA12 4.5 12.6 1.0 O3P A:POA600 4.5 54.4 1.0 O2 A:POA600 4.6 40.1 1.0 C1 A:POA600 4.7 44.9 1.0 N A:THR187 4.7 15.6 1.0 CB A:THR187 4.8 13.2 1.0 N A:ALA14 4.8 11.1 1.0 CB A:ASP186 4.8 17.7 1.0 CA A:GLY50 4.8 14.1 1.0 C A:ALA12 4.8 11.1 1.0 CB A:THR16 4.9 13.0 1.0 CB A:ASP190 4.9 11.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Phosphonoacetaldehyde Hydrolase D12A Mutant Complexed with Magnesium and Substrate Phosphonoacetaldehyde


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Phosphonoacetaldehyde Hydrolase D12A Mutant Complexed with Magnesium and Substrate Phosphonoacetaldehyde within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:48.5 occ:1.00 O1P B:POA700 2.2 56.6 1.0 O2P B:POA700 2.3 57.0 1.0 OD2 B:ASP190 2.5 21.6 1.0 O B:HOH717 2.6 25.6 1.0 P B:POA700 2.6 53.4 1.0 OD1 B:ASP186 2.9 26.8 1.0 O3P B:POA700 3.3 55.8 1.0 O B:ALA14 3.3 30.2 1.0 O B:HOH702 3.3 24.4 1.0 CG B:ASP190 3.5 21.8 1.0 CG2 B:THR187 3.5 23.3 1.0 CB B:ALA12 3.6 31.8 1.0 OD1 B:ASP190 3.6 23.9 1.0 CG B:ASP186 3.9 26.7 1.0 NH1 B:ARG160 4.0 18.9 1.0 OG1 B:THR187 4.1 24.8 1.0 OD2 B:ASP186 4.2 25.8 1.0 C1 B:POA700 4.4 53.3 1.0 CB B:THR187 4.4 24.2 1.0 C B:ALA14 4.5 29.3 1.0 O B:HOH759 4.5 20.4 1.0 CA B:GLY50 4.5 20.9 1.0 CZ B:ARG160 4.6 18.6 1.0 OG1 B:THR16 4.7 35.0 1.0 N B:THR187 4.7 26.3 1.0 CA B:ALA12 4.7 33.0 1.0 N B:ASP186 4.7 26.7 1.0 N B:TRP13 4.8 29.3 1.0 CB B:ASP190 4.9 23.8 1.0 NH2 B:ARG160 4.9 22.3 1.0 C2 B:POA700 5.0 49.5 1.0

G.Zhang, M.C.Morais, J.Dai, W.Zhang, D.Dunaway-Mariano, K.N.Allen. Investigation of Metal Ion Binding in Phosphonoacetaldehyde Hydrolase Identifies Sequence Markers For Metal-Activated Enzymes of the Had Enzyme Superfamily Biochemistry V. 43 4990 2004.
ISSN: ISSN 0006-2960
PubMed: 15109258
DOI: 10.1021/BI036309N