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Magnesium in PDB 2yhy: Structure of N-Acetylmannosamine Kinase in Complex with N- Acetylmannosamine and Adp

Enzymatic activity of Structure of N-Acetylmannosamine Kinase in Complex with N- Acetylmannosamine and Adp

All present enzymatic activity of Structure of N-Acetylmannosamine Kinase in Complex with N- Acetylmannosamine and Adp:
2.7.1.60;

Protein crystallography data

The structure of Structure of N-Acetylmannosamine Kinase in Complex with N- Acetylmannosamine and Adp, PDB code: 2yhy was solved by J.Martinez, L.D.Nguyen, E.Tauberger, S.Hinderlich, W.Reutter, H.Fan, W.Saenger, S.Moniot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.26 / 1.82
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 90.380, 90.380, 101.160, 90.00, 90.00, 90.00
R / Rfree (%) 15.228 / 18.163

Other elements in 2yhy:

The structure of Structure of N-Acetylmannosamine Kinase in Complex with N- Acetylmannosamine and Adp also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Calcium (Ca) 2 atoms
Zinc (Zn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of N-Acetylmannosamine Kinase in Complex with N- Acetylmannosamine and Adp (pdb code 2yhy). 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 Structure of N-Acetylmannosamine Kinase in Complex with N- Acetylmannosamine and Adp, PDB code: 2yhy:

Magnesium binding site 1 out of 1 in 2yhy

Go back to Magnesium Binding Sites List in 2yhy
Magnesium binding site 1 out of 1 in the Structure of N-Acetylmannosamine Kinase in Complex with N- Acetylmannosamine and Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of N-Acetylmannosamine Kinase in Complex with N- Acetylmannosamine and Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1723

b:28.2
occ:1.00
 O A:HOH2005 2.0 31.7 1.0
O1B A:ADP1727 2.2 38.5 0.7
OD2 A:ASP413 2.3 21.9 1.0
O A:HOH2004 2.3 19.8 1.0
O A:HOH2009 2.6 49.6 1.0
O A:HOH2003 2.7 35.0 1.0
CG A:ASP413 3.3 22.2 1.0
PB A:ADP1727 3.6 40.5 0.7
OD1 A:ASP413 3.7 20.2 1.0
O A:HOH2006 3.9 24.1 1.0
O2B A:ADP1727 4.2 28.9 0.7
O1A A:ADP1727 4.3 46.4 0.7
O A:HOH2193 4.3 25.9 1.0
O3A A:ADP1727 4.4 41.4 0.7
NH1 A:ARG420 4.4 46.0 1.0
CA A:GLY415 4.5 29.6 1.0
CB A:ALA705 4.5 19.7 1.0
PA A:ADP1727 4.6 47.8 0.7
O3B A:ADP1727 4.6 38.8 0.7
CB A:ASP413 4.7 17.9 1.0
N A:GLY415 4.7 27.9 1.0
O2A A:ADP1727 4.9 48.5 0.7
OD2 A:ASP517 4.9 20.0 1.0

Reference:

J.Martinez, L.D.Nguyen, E.Tauberger, S.Hinderlich, W.Reutter, H.Fan, W.Saenger, S.Moniot. Crystal Structures of N-Acetylmannosamine Kinase Provide Insights Into Enzyme Specificity and Inhibition J.Biol.Chem. V. 287 13656 2012.
ISSN: ISSN 0021-9258
PubMed: 22343627
DOI: 10.1074/JBC.M111.318170
Page generated: Mon Dec 14 07:48:50 2020

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