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Magnesium in PDB 7jhn: Structure of Human Beta 1,3-N-Acetylglucosaminyltransferase 2 with Udp and Trisaccharide Glcnac-BETA1-3GAL-BETA1-4GLCNAC

Enzymatic activity of Structure of Human Beta 1,3-N-Acetylglucosaminyltransferase 2 with Udp and Trisaccharide Glcnac-BETA1-3GAL-BETA1-4GLCNAC

All present enzymatic activity of Structure of Human Beta 1,3-N-Acetylglucosaminyltransferase 2 with Udp and Trisaccharide Glcnac-BETA1-3GAL-BETA1-4GLCNAC:
2.4.1.149;

Protein crystallography data

The structure of Structure of Human Beta 1,3-N-Acetylglucosaminyltransferase 2 with Udp and Trisaccharide Glcnac-BETA1-3GAL-BETA1-4GLCNAC, PDB code: 7jhn was solved by Y.Hao, X.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.89 / 2.20
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 82.916, 76.865, 66.786, 90.00, 105.82, 90.00
R / Rfree (%) 19.6 / 25.5

Other elements in 7jhn:

The structure of Structure of Human Beta 1,3-N-Acetylglucosaminyltransferase 2 with Udp and Trisaccharide Glcnac-BETA1-3GAL-BETA1-4GLCNAC also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Human Beta 1,3-N-Acetylglucosaminyltransferase 2 with Udp and Trisaccharide Glcnac-BETA1-3GAL-BETA1-4GLCNAC (pdb code 7jhn). 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 Human Beta 1,3-N-Acetylglucosaminyltransferase 2 with Udp and Trisaccharide Glcnac-BETA1-3GAL-BETA1-4GLCNAC, PDB code: 7jhn:

Magnesium binding site 1 out of 1 in 7jhn

Go back to Magnesium Binding Sites List in 7jhn
Magnesium binding site 1 out of 1 in the Structure of Human Beta 1,3-N-Acetylglucosaminyltransferase 2 with Udp and Trisaccharide Glcnac-BETA1-3GAL-BETA1-4GLCNAC


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Beta 1,3-N-Acetylglucosaminyltransferase 2 with Udp and Trisaccharide Glcnac-BETA1-3GAL-BETA1-4GLCNAC within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:37.8
occ:1.00
 O A:HOH504 2.1 28.0 1.0
OD2 A:ASP247 2.1 32.2 1.0
O2A A:UDP403 2.2 45.5 1.0
O3B A:UDP403 2.3 54.3 1.0
NE2 A:HIS376 2.6 29.7 1.0
O A:HOH557 2.6 41.4 1.0
CG A:ASP247 2.9 20.7 1.0
OD1 A:ASP247 2.9 18.3 1.0
CD2 A:HIS376 3.3 35.6 1.0
PB A:UDP403 3.4 52.2 1.0
PA A:UDP403 3.5 32.7 1.0
CE1 A:HIS376 3.6 32.9 1.0
O2B A:UDP403 3.7 54.9 1.0
O3A A:UDP403 3.9 44.6 1.0
O5' A:UDP403 4.2 36.2 1.0
OD1 A:ASP245 4.3 37.6 1.0
CB A:ASP247 4.3 22.6 1.0
C5' A:UDP403 4.4 28.9 1.0
O1A A:UDP403 4.5 36.5 1.0
CG A:HIS376 4.6 30.9 1.0
ND1 A:HIS376 4.7 45.2 1.0
O1B A:UDP403 4.7 61.6 1.0
C3' A:UDP403 4.9 23.9 1.0
CB A:SER377 4.9 24.6 1.0
CB A:ASP245 4.9 17.8 1.0
CG A:ASP245 4.9 31.4 1.0

Reference:

Y.Hao, A.Crequer-Grandhomme, N.Javier, A.Singh, H.Chen, P.Manzanillo, M.C.Lo, X.Huang. Structures and Mechanism of Human Glycosyltransferase Beta 1,3-N-Acetylglucosaminyltransferase 2 (B3GNT2), An Important Player in Immune Homeostasis. J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
PubMed: 33158990
DOI: 10.1074/JBC.RA120.015306
Page generated: Wed Oct 2 21:52:30 2024

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