Magnesium in PDB 2x5f: Crystal Structure of the Methicillin-Resistant Staphylococcus Aureus SAR2028, An ASPARTATE_TYROSINE_PHENYLALANINE Pyridoxal-5'-Phosphate Dependent Aminotransferase

The structure of Crystal Structure of the Methicillin-Resistant Staphylococcus Aureus SAR2028, An ASPARTATE_TYROSINE_PHENYLALANINE Pyridoxal-5'-Phosphate Dependent Aminotransferase, PDB code: 2x5f was solved by M.Oke, L.G.Carter, K.A.Johnson, H.Liu, S.A.Mcmahon, M.F.White, J.H.Naismith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.24 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	82.780, 89.990, 104.910, 90.00, 90.00, 90.00
R / Rfree (%)	19.099 / 21.049

The binding sites of Magnesium atom in the Crystal Structure of the Methicillin-Resistant Staphylococcus Aureus SAR2028, An ASPARTATE_TYROSINE_PHENYLALANINE Pyridoxal-5'-Phosphate Dependent Aminotransferase (pdb code 2x5f). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Methicillin-Resistant Staphylococcus Aureus SAR2028, An ASPARTATE_TYROSINE_PHENYLALANINE Pyridoxal-5'-Phosphate Dependent Aminotransferase, PDB code: 2x5f:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Methicillin-Resistant Staphylococcus Aureus SAR2028, An ASPARTATE_TYROSINE_PHENYLALANINE Pyridoxal-5'-Phosphate Dependent Aminotransferase


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 Methicillin-Resistant Staphylococcus Aureus SAR2028, An ASPARTATE_TYROSINE_PHENYLALANINE Pyridoxal-5'-Phosphate Dependent Aminotransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1429 b:16.6 occ:1.00 O B:VAL132 2.1 19.1 1.0 O B:GLY128 2.2 17.2 1.0 OD1 B:ASN156 2.3 21.6 1.0 O B:HOH2040 2.3 4.4 1.0 O B:HOH2053 2.6 3.8 1.0 C B:GLY128 3.2 16.2 1.0 CG B:ASN156 3.3 18.9 1.0 C B:VAL132 3.3 19.8 1.0 CB B:ASN156 3.8 18.7 1.0 O B:HOH2039 3.9 16.3 1.0 CB B:VAL132 3.9 19.0 1.0 CA B:VAL132 3.9 18.8 1.0 N B:ASP129 4.0 15.4 1.0 CA B:ASP129 4.1 16.5 1.0 N B:VAL132 4.1 18.4 1.0 O B:ASP129 4.1 17.6 1.0 CA B:GLY128 4.2 15.8 1.0 C B:ASP129 4.3 16.1 1.0 ND2 B:ASN156 4.3 16.8 1.0 N B:ASN133 4.4 20.7 1.0 O B:HOH2007 4.4 8.8 1.0 CA B:ASN156 4.5 19.5 1.0 O B:ASN156 4.5 19.9 1.0 CG1 B:VAL132 4.5 18.6 1.0 CB B:SER24 4.6 18.6 1.0 CA B:ASN133 4.7 21.9 1.0 OG B:SER24 4.8 16.4 1.0 C B:ASN156 5.0 20.1 1.0

M.Oke, L.G.Carter, K.A.Johnson, H.Liu, S.A.Mcmahon, X.Yan, M.Kerou, N.D.Weikart, N.Kadi, M.A.Sheikh, S.Schmelz, M.Dorward, M.Zawadzki, C.Cozens, H.Falconer, H.Powers, I.M.Overton, C.A.J.Van Niekerk, X.Peng, P.Patel, R.A.Garrett, D.Prangishvili, C.H.Botting, P.J.Coote, D.T.F.Dryden, G.J.Barton, U.Schwarz-Linek, G.L.Challis, G.L.Taylor, M.F.White, J.H.Naismith. The Scottish Structural Proteomics Facility: Targets, Methods and Outputs. J.Struct.Funct.Genom. V. 11 167 2010.
ISSN: ISSN 1345-711X
PubMed: 20419351
DOI: 10.1007/S10969-010-9090-Y