Magnesium in PDB 2qs8: Crystal Structure of A Xaa-Pro Dipeptidase with Bound Methionine in the Active Site

The structure of Crystal Structure of A Xaa-Pro Dipeptidase with Bound Methionine in the Active Site, PDB code: 2qs8 was solved by D.Kumaran, S.K.Burley, S.Swaminathan, New York Sgx Research Center Forstructural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.81 / 2.33
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	144.846, 144.846, 101.029, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 23.4

The binding sites of Magnesium atom in the Crystal Structure of A Xaa-Pro Dipeptidase with Bound Methionine in the Active Site (pdb code 2qs8). 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 A Xaa-Pro Dipeptidase with Bound Methionine in the Active Site, PDB code: 2qs8:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of A Xaa-Pro Dipeptidase with Bound Methionine in the Active Site


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 A Xaa-Pro Dipeptidase with Bound Methionine in the Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg500 b:29.6 occ:1.00 NE2 A:HIS71 2.2 25.7 1.0 NE2 A:HIS69 2.4 26.1 1.0 OD1 A:ASP328 2.6 23.8 1.0 O A:HOH677 3.0 34.0 1.0 O A:HOH751 3.0 33.9 1.0 CE1 A:HIS71 3.1 25.7 1.0 CD2 A:HIS71 3.2 22.3 1.0 CG A:ASP328 3.3 25.4 1.0 CD2 A:HIS69 3.4 25.7 1.0 CE1 A:HIS69 3.4 24.8 1.0 OD2 A:ASP328 3.5 25.0 1.0 N A:MET600 3.9 39.6 1.0 ND1 A:HIS71 4.2 23.6 1.0 NZ A:LYS194 4.3 27.2 1.0 CG A:HIS71 4.3 23.0 1.0 NE2 A:HIS255 4.4 23.1 1.0 ND1 A:HIS69 4.5 26.4 1.0 CG A:HIS69 4.5 26.0 1.0 CE1 A:HIS255 4.6 22.5 1.0 CB A:ASP328 4.6 24.0 1.0 O A:HOH621 4.7 30.8 1.0 CA A:MET600 4.9 38.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of A Xaa-Pro Dipeptidase with Bound Methionine in the Active Site


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 A Xaa-Pro Dipeptidase with Bound Methionine in the Active Site within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg500 b:32.2 occ:1.00 NE2 B:HIS71 2.1 26.1 1.0 O B:HOH834 2.1 33.4 1.0 NE2 B:HIS69 2.3 27.2 1.0 OD1 B:ASP328 2.5 26.6 1.0 CE1 B:HIS71 2.8 26.1 1.0 O B:HOH768 3.0 33.5 1.0 CD2 B:HIS71 3.2 24.1 1.0 CD2 B:HIS69 3.2 27.8 1.0 CG B:ASP328 3.3 27.0 1.0 NZ B:LYS194 3.3 38.2 1.0 CE1 B:HIS69 3.3 27.8 1.0 OD2 B:ASP328 3.6 28.3 1.0 ND1 B:HIS71 4.0 24.3 1.0 N B:MET700 4.1 42.6 1.0 CG B:HIS71 4.2 22.7 1.0 NE2 B:HIS255 4.3 28.0 1.0 CG B:HIS69 4.4 26.8 1.0 ND1 B:HIS69 4.4 28.4 1.0 CE1 B:HIS255 4.4 28.4 1.0 CB B:ASP328 4.5 26.0 1.0 CE B:LYS194 4.7 36.6 1.0 CG2 B:VAL113 4.8 23.1 1.0 CA B:ASP328 4.9 24.6 1.0 O B:HOH765 4.9 36.0 1.0 O B:VAL113 4.9 24.5 1.0 CA B:MET700 5.0 40.1 1.0

D.F.Xiang, C.Xu, D.Kumaran, A.C.Brown, J.M.Sauder, S.K.Burley, S.Swaminathan, F.M.Raushel. Functional Annotation of Two New Carboxypeptidases From the Amidohydrolase Superfamily of Enzymes. Biochemistry V. 48 4567 2009.
ISSN: ISSN 0006-2960
PubMed: 19358546
DOI: 10.1021/BI900453U