Magnesium in PDB 1h74: Crystal Structure of Homoserine Kinase Complexed with Ile

All present enzymatic activity of Crystal Structure of Homoserine Kinase Complexed with Ile:
2.7.1.39;

The structure of Crystal Structure of Homoserine Kinase Complexed with Ile, PDB code: 1h74 was solved by S.S.Krishna, T.Zhou, M.Daugherty, A.L.Osterman, H.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.993, 128.721, 109.423, 90.00, 105.57, 90.00
R / Rfree (%)	21 / 23.8

The binding sites of Magnesium atom in the Crystal Structure of Homoserine Kinase Complexed with Ile (pdb code 1h74). 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 Homoserine Kinase Complexed with Ile, PDB code: 1h74:

Magnesium binding site 1 out of 1 in the Crystal Structure of Homoserine Kinase Complexed with Ile


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 Homoserine Kinase Complexed with Ile within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg600 b:87.8 occ:1.00 O2B B:AGS400 2.4 97.5 1.0 O3G B:AGS400 3.0 0.6 1.0 OE1 B:GLU130 3.0 95.0 1.0 O2G B:AGS400 3.0 0.8 1.0 CB B:SER98 3.1 61.5 1.0 OE2 B:GLU130 3.2 94.8 1.0 PG B:AGS400 3.4 0.6 1.0 CD B:GLU130 3.4 95.0 1.0 PB B:AGS400 3.7 97.7 1.0 O3B B:AGS400 3.8 0.5 1.0 N B:ALA99 3.8 60.2 1.0 O2A B:AGS400 3.9 95.8 1.0 OG B:SER98 3.9 66.1 1.0 O B:HOH2074 4.0 72.0 1.0 CA B:SER98 4.1 60.5 1.0 N B:SER98 4.1 59.2 1.0 O3A B:AGS400 4.4 96.5 1.0 C B:SER98 4.4 60.7 1.0 O5' B:AGS400 4.4 92.5 1.0 CA B:GLY96 4.5 50.5 1.0 PA B:AGS400 4.5 94.8 1.0 CB B:ALA99 4.6 59.7 1.0 C B:GLY96 4.7 52.6 1.0 CA B:ALA99 4.7 58.8 1.0 CG B:GLU130 4.9 94.7 1.0 O1B B:AGS400 4.9 97.7 1.0 N B:SER97 4.9 55.0 1.0

S.S.Krishna, T.Zhou, M.Daugherty, A.L.Osterman, H.Zhang. Structural Basis For the Catalysis and Substrate Specificity of Homoserine Kinase Biochemistry V. 40 10810 2001.
ISSN: ISSN 0006-2960
PubMed: 11535056
DOI: 10.1021/BI010851Z