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Magnesium in PDB 4ocp: N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac-1- Phosphate and Adp

Enzymatic activity of N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac-1- Phosphate and Adp

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

Protein crystallography data

The structure of N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac-1- Phosphate and Adp, PDB code: 4ocp 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) 28.06 / 1.94
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.142, 79.236, 97.791, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 21.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac-1- Phosphate and Adp (pdb code 4ocp). 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 N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac-1- Phosphate and Adp, PDB code: 4ocp:

Magnesium binding site 1 out of 1 in 4ocp

Go back to Magnesium Binding Sites List in 4ocp
Magnesium binding site 1 out of 1 in the N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac-1- Phosphate and Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of N-Acetylhexosamine 1-Phosphate Kinase in Complex with Glcnac-1- Phosphate and Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:24.2
occ:1.00
OD2 A:ASP228 2.0 21.0 1.0
O A:HOH513 2.1 27.3 1.0
O1A A:ADP402 2.1 23.3 1.0
O1B A:ADP402 2.2 24.9 1.0
OP1 A:GN1401 2.2 22.6 1.0
OD1 A:ASN213 2.2 22.6 1.0
CG A:ASP228 3.1 20.3 1.0
CG A:ASN213 3.2 21.1 1.0
PA A:ADP402 3.3 24.0 1.0
PB A:ADP402 3.3 23.7 1.0
P A:GN1401 3.4 22.2 1.0
O A:HOH510 3.5 21.3 1.0
ND2 A:ASN213 3.5 21.1 1.0
CB A:ASP228 3.6 19.5 1.0
O3A A:ADP402 3.6 23.5 1.0
OP2 A:GN1401 3.7 21.1 1.0
O3B A:ADP402 3.9 26.1 1.0
OP3 A:GN1401 4.0 21.0 1.0
OD1 A:ASP228 4.1 20.5 1.0
OD2 A:ASP208 4.2 23.4 1.0
O2A A:ADP402 4.3 22.8 1.0
O3' A:ADP402 4.3 23.9 1.0
CE A:LYS210 4.4 22.1 1.0
O5' A:ADP402 4.4 22.1 1.0
OD1 A:ASN212 4.4 24.7 1.0
CA A:GLY30 4.5 24.1 1.0
CB A:ASN213 4.6 21.5 1.0
C5' A:ADP402 4.6 22.0 1.0
O2B A:ADP402 4.6 23.6 1.0
O1' A:GN1401 4.7 19.0 1.0
C3' A:ADP402 4.8 22.6 1.0

Reference:

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
Page generated: Tue Aug 20 00:46:57 2024

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