Calcium in PDB 2ogy: ASN199ALA Mutant of the 5-Methyltetrahydrofolate Corrinoid/Iron Sulfur Protein Methyltransferase Complexed with Methyltetrahydrofolate to 2.3 Angstrom Resolution

The structure of ASN199ALA Mutant of the 5-Methyltetrahydrofolate Corrinoid/Iron Sulfur Protein Methyltransferase Complexed with Methyltetrahydrofolate to 2.3 Angstrom Resolution, PDB code: 2ogy was solved by T.I.Doukov, C.L.Drennan, H.Hemmi, S.W.Ragsdale, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.19 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.772, 78.673, 135.857, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 23.4

The binding sites of Calcium atom in the ASN199ALA Mutant of the 5-Methyltetrahydrofolate Corrinoid/Iron Sulfur Protein Methyltransferase Complexed with Methyltetrahydrofolate to 2.3 Angstrom Resolution (pdb code 2ogy). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the ASN199ALA Mutant of the 5-Methyltetrahydrofolate Corrinoid/Iron Sulfur Protein Methyltransferase Complexed with Methyltetrahydrofolate to 2.3 Angstrom Resolution, PDB code: 2ogy:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the ASN199ALA Mutant of the 5-Methyltetrahydrofolate Corrinoid/Iron Sulfur Protein Methyltransferase Complexed with Methyltetrahydrofolate to 2.3 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of ASN199ALA Mutant of the 5-Methyltetrahydrofolate Corrinoid/Iron Sulfur Protein Methyltransferase Complexed with Methyltetrahydrofolate to 2.3 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca3001 b:15.9 occ:1.00 OD1 A:ASP224 2.4 9.4 1.0 O A:GLY222 2.4 8.2 1.0 O A:HOH3092 2.5 9.3 1.0 OD2 A:ASP224 2.5 9.6 1.0 O A:HOH3032 2.5 12.1 1.0 O A:HOH3127 2.6 14.7 1.0 O A:HOH3111 2.7 12.5 1.0 CG A:ASP224 2.8 10.6 1.0 O A:HOH3027 2.9 24.7 1.0 C A:GLY222 3.5 8.8 1.0 CA A:GLY222 3.9 7.9 1.0 CB A:ASP224 4.2 8.3 1.0 O A:HOH3131 4.4 23.7 1.0 O A:HOH3017 4.5 8.2 1.0 N A:ASP224 4.6 8.2 1.0 OG1 A:THR193 4.6 7.7 1.0 C A:LEU223 4.6 8.1 1.0 N A:LEU223 4.7 8.6 1.0 O A:HOH3023 4.7 6.9 1.0 O A:HOH3012 4.7 11.2 1.0 CA A:ASP224 4.8 8.0 1.0 O A:LEU223 4.9 10.2 1.0 O A:HOH3035 4.9 18.9 1.0 O A:PRO191 4.9 10.2 1.0

Calcium binding site 2 out of 2 in the ASN199ALA Mutant of the 5-Methyltetrahydrofolate Corrinoid/Iron Sulfur Protein Methyltransferase Complexed with Methyltetrahydrofolate to 2.3 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of ASN199ALA Mutant of the 5-Methyltetrahydrofolate Corrinoid/Iron Sulfur Protein Methyltransferase Complexed with Methyltetrahydrofolate to 2.3 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca4001 b:21.6 occ:1.00 O B:HOH4048 2.3 27.8 1.0 O B:HOH4050 2.5 19.2 1.0 OD1 B:ASP224 2.5 12.4 1.0 O B:GLY222 2.5 10.4 1.0 OD2 B:ASP224 2.6 9.0 1.0 O B:HOH4062 2.7 15.6 1.0 O B:HOH4151 2.8 13.4 1.0 CG B:ASP224 2.9 10.8 1.0 O B:HOH4104 3.0 18.5 1.0 C B:GLY222 3.6 9.6 1.0 CA B:GLY222 4.0 9.0 1.0 O B:HOH4102 4.0 19.1 1.0 CB B:ASP224 4.3 8.2 1.0 OG1 B:THR193 4.5 6.7 1.0 O B:HOH4038 4.6 20.5 1.0 O B:HOH4034 4.7 12.1 1.0 N B:ASP224 4.7 9.6 1.0 C B:LEU223 4.7 8.8 1.0 O B:PRO191 4.7 11.2 1.0 N B:LEU223 4.8 10.1 1.0 CA B:ASP224 4.9 8.4 1.0 O B:LEU223 4.9 9.6 1.0 O B:HOH4009 4.9 5.4 1.0

T.I.Doukov, H.Hemmi, C.L.Drennan, S.W.Ragsdale. Structural and Kinetic Evidence For An Extended Hydrogen-Bonding Network in Catalysis of Methyl Group Transfer. Role of An Active Site Asparagine Residue in Activation of Methyl Transfer By Methyltransferases. J.Biol.Chem. V. 282 6609 2007.
ISSN: ISSN 0021-9258
PubMed: 17172470
DOI: 10.1074/JBC.M609828200