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Magnesium in PDB 6fwz: Crystal Structure of Human Udp-N-Acetylglucosamine-Dolichyl-Phosphate N-Acetylglucosaminephosphotransferase (DPAGT1) (V264G Mutant) in Complex with Udp-GlcnacEnzymatic activity of Crystal Structure of Human Udp-N-Acetylglucosamine-Dolichyl-Phosphate N-Acetylglucosaminephosphotransferase (DPAGT1) (V264G Mutant) in Complex with Udp-Glcnac
All present enzymatic activity of Crystal Structure of Human Udp-N-Acetylglucosamine-Dolichyl-Phosphate N-Acetylglucosaminephosphotransferase (DPAGT1) (V264G Mutant) in Complex with Udp-Glcnac:
2.7.8.15; Protein crystallography data
The structure of Crystal Structure of Human Udp-N-Acetylglucosamine-Dolichyl-Phosphate N-Acetylglucosaminephosphotransferase (DPAGT1) (V264G Mutant) in Complex with Udp-Glcnac, PDB code: 6fwz
was solved by
A.C.W.Pike,
Y.Y.Dong,
A.Chu,
A.Tessitore,
S.Goubin,
L.Dong,
S.Mukhopadhyay,
P.Mahajan,
R.Chalk,
G.Berridge,
D.Wang,
K.Kupinska,
K.Belaya,
D.Beeson,
N.Burgess-Brown,
A.M.Edwards,
C.H.Arrowsmith,
C.Bountra,
E.P.Carpenter,
Structural Genomics Consortium (Sgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Human Udp-N-Acetylglucosamine-Dolichyl-Phosphate N-Acetylglucosaminephosphotransferase (DPAGT1) (V264G Mutant) in Complex with Udp-Glcnac
(pdb code 6fwz). 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 Human Udp-N-Acetylglucosamine-Dolichyl-Phosphate N-Acetylglucosaminephosphotransferase (DPAGT1) (V264G Mutant) in Complex with Udp-Glcnac, PDB code: 6fwz: Magnesium binding site 1 out of 1 in 6fwzGo back to Magnesium Binding Sites List in 6fwz
Magnesium binding site 1 out
of 1 in the Crystal Structure of Human Udp-N-Acetylglucosamine-Dolichyl-Phosphate N-Acetylglucosaminephosphotransferase (DPAGT1) (V264G Mutant) in Complex with Udp-Glcnac
Mono view Stereo pair view
Reference:
Y.Y.Dong,
H.Wang,
A.C.W.Pike,
S.A.Cochrane,
S.Hamedzadeh,
F.J.Wyszynski,
S.R.Bushell,
S.F.Royer,
D.A.Widdick,
A.Sajid,
H.I.Boshoff,
Y.Park,
R.Lucas,
W.M.Liu,
S.S.Lee,
T.Machida,
L.Minall,
S.Mehmood,
K.Belaya,
W.W.Liu,
A.Chu,
L.Shrestha,
S.M.M.Mukhopadhyay,
C.Strain-Damerell,
R.Chalk,
N.A.Burgess-Brown,
M.J.Bibb,
C.E.Barry Iii,
C.V.Robinson,
D.Beeson,
B.G.Davis,
E.P.Carpenter.
Structures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance Tb Antibiotic Design. Cell V. 175 1045 2018.
Page generated: Mon Dec 14 22:43:16 2020
ISSN: ISSN 1097-4172 PubMed: 30388443 DOI: 10.1016/J.CELL.2018.10.037 |
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