Sodium in PDB 4ocj: N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac

All present enzymatic activity of N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac:
2.7.1.162;

The structure of N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac, PDB code: 4ocj was solved by T.L.Li, K.C.Wang, S.Y.Lyu, Y.C.Liu, C.Y.Chang, C.J.Wu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.60 / 1.57
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.367, 79.510, 98.122, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / 18.3

The binding sites of Sodium atom in the N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac (pdb code 4ocj). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac, PDB code: 4ocj:

Sodium binding site 1 out of 1 in the N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac within 5.0Å range: probe atom residue distance (Å) B Occ A:Na402 b:20.0 occ:1.00 O A:HOH1028 2.0 34.4 1.0 O A:HOH1029 2.0 33.3 1.0 O A:HOH1031 2.0 41.9 1.0 O A:HOH1030 2.1 35.3 1.0 NE2 A:HIS154 2.5 24.1 1.0 CD2 A:HIS154 3.3 21.9 1.0 CE1 A:HIS154 3.6 23.9 1.0 OD2 A:ASP158 3.8 17.7 1.0 O A:HOH960 3.9 31.2 1.0 OD1 A:ASP158 4.0 19.5 1.0 O A:HOH720 4.3 34.2 1.0 CG A:ASP158 4.4 16.9 1.0 CG A:HIS154 4.5 19.7 1.0 ND1 A:HIS154 4.6 23.4 1.0 ND1 A:HIS148 4.7 25.4 1.0

K.C.Wang, S.Y.Lyu, Y.C.Liu, C.Y.Chang, C.J.Wu, T.L.Li. Insights Into the Binding Specificity and Catalytic Mechanism of N-Acetylhexosamine 1-Phosphate Kinases Through Multiple Reaction Complexes. Acta Crystallogr.,Sect.D V. 70 1401 2014.
ISSN: ISSN 0907-4449
PubMed: 24816108
DOI: 10.1107/S1399004714004209