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Manganese in PDB 7e9s: Archaeal Oligosaccharyltransferase Aglb From Archaeoglobus Fulgidus in Complex with An Inhibitory Peptide and A Dolichol-Phosphate

Enzymatic activity of Archaeal Oligosaccharyltransferase Aglb From Archaeoglobus Fulgidus in Complex with An Inhibitory Peptide and A Dolichol-Phosphate

All present enzymatic activity of Archaeal Oligosaccharyltransferase Aglb From Archaeoglobus Fulgidus in Complex with An Inhibitory Peptide and A Dolichol-Phosphate:
2.4.99.21;

Protein crystallography data

The structure of Archaeal Oligosaccharyltransferase Aglb From Archaeoglobus Fulgidus in Complex with An Inhibitory Peptide and A Dolichol-Phosphate, PDB code: 7e9s was solved by Y.Taguchi, K.Hirata, D.Kohda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.84 / 2.70
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 345.74, 48.69, 63.56, 90, 90, 90
R / Rfree (%) 21.5 / 25.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Archaeal Oligosaccharyltransferase Aglb From Archaeoglobus Fulgidus in Complex with An Inhibitory Peptide and A Dolichol-Phosphate (pdb code 7e9s). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Archaeal Oligosaccharyltransferase Aglb From Archaeoglobus Fulgidus in Complex with An Inhibitory Peptide and A Dolichol-Phosphate, PDB code: 7e9s:

Manganese binding site 1 out of 1 in 7e9s

Go back to Manganese Binding Sites List in 7e9s
Manganese binding site 1 out of 1 in the Archaeal Oligosaccharyltransferase Aglb From Archaeoglobus Fulgidus in Complex with An Inhibitory Peptide and A Dolichol-Phosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Archaeal Oligosaccharyltransferase Aglb From Archaeoglobus Fulgidus in Complex with An Inhibitory Peptide and A Dolichol-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn901

b:73.6
occ:1.00
 O A:HOH1005 2.0 64.4 1.0
OD2 A:ASP161 2.1 72.5 1.0
O A:HOH1009 2.1 59.6 1.0
NE2 A:HIS163 2.3 73.9 1.0
O A:HOH1002 2.4 71.6 1.0
OD2 A:ASP47 2.4 84.1 1.0
CD2 A:HIS163 3.2 70.2 1.0
CG A:ASP161 3.3 68.3 1.0
CE1 A:HIS163 3.3 71.6 1.0
CG A:ASP47 3.4 66.8 1.0
CB A:ASP47 3.7 63.1 1.0
OD1 A:ASP161 3.8 69.1 1.0
CG A:HIS163 4.3 69.6 1.0
OE1 A:GLU360 4.4 82.2 1.0
ND1 A:HIS163 4.4 70.3 1.0
CB A:ASP161 4.5 56.3 1.0
O63 A:J06902 4.5 84.1 1.0
CB B:DAB4 4.5 81.2 1.0
OD1 A:ASP47 4.6 63.6 1.0
O64 A:J06902 4.6 81.1 1.0
NH1 A:ARG154 4.6 77.5 1.0
ND B:DAB4 4.7 95.8 1.0
P62 A:J06902 4.8 88.2 1.0
OE2 A:GLU360 5.0 93.9 1.0

Reference:

Y.Taguchi, T.Yamasaki, M.Ishikawa, Y.Kawasaki, R.Yukimura, M.Mitani, K.Hirata, D.Kohda. The Structure of An Archaeal Oligosaccharyltransferase Provides Insight Into the Strict Exclusion of Proline From the N-Glycosylation Sequon. Commun Biol V. 4 941 2021.
ISSN: ESSN 2399-3642
PubMed: 34354228
DOI: 10.1038/S42003-021-02473-8
Page generated: Sun Oct 6 08:29:17 2024

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