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Zinc in PDB 3waj: Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) Complex with Zn and Sulfate

Enzymatic activity of Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) Complex with Zn and Sulfate

All present enzymatic activity of Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) Complex with Zn and Sulfate:
2.4.1.119;

Protein crystallography data

The structure of Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) Complex with Zn and Sulfate, PDB code: 3waj was solved by S.Matsumoto, A.Shimada, D.Kohda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.81 / 2.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 234.195, 108.961, 56.069, 90.00, 96.08, 90.00
R / Rfree (%) 18.2 / 21.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) Complex with Zn and Sulfate (pdb code 3waj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) Complex with Zn and Sulfate, PDB code: 3waj:

Zinc binding site 1 out of 1 in 3waj

Go back to Zinc Binding Sites List in 3waj
Zinc binding site 1 out of 1 in the Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) Complex with Zn and Sulfate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) Complex with Zn and Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:40.2
occ:1.00
 NE2 A:HIS163 2.2 35.9 1.0
O A:HOH1122 2.2 71.7 1.0
OD2 A:ASP161 2.2 51.1 1.0
O A:HOH1001 2.3 38.0 1.0
O A:HOH1137 2.5 39.0 1.0
OD2 A:ASP47 2.8 43.4 1.0
CD2 A:HIS163 3.1 32.2 1.0
CG A:ASP161 3.1 38.4 1.0
CE1 A:HIS163 3.2 36.2 1.0
OD1 A:ASP161 3.5 38.7 1.0
CG A:ASP47 3.7 43.2 1.0
CB A:ASP47 3.9 41.8 1.0
O A:HOH1133 4.2 51.7 1.0
CG A:HIS163 4.2 34.8 1.0
ND1 A:HIS163 4.2 32.0 1.0
O1 A:SO4902 4.4 50.6 1.0
CB A:ASP161 4.4 33.1 1.0
O3 A:SO4902 4.6 60.2 1.0
O A:HOH1136 4.8 23.2 1.0
O A:HOH1067 4.8 43.1 1.0
CE2 A:PHE159 4.9 31.3 1.0
OD1 A:ASP47 4.9 37.1 1.0
NE2 A:HIS162 4.9 38.2 1.0

Reference:

S.Matsumoto, A.Shimada, J.Nyirenda, M.Igura, Y.Kawano, D.Kohda. Crystal Structures of An Archaeal Oligosaccharyltransferase Provide Insights Into the Catalytic Cycle of N-Linked Protein Glycosylation Proc.Natl.Acad.Sci.Usa V. 110 17868 2013.
ISSN: ISSN 0027-8424
PubMed: 24127570
DOI: 10.1073/PNAS.1309777110
Page generated: Sat Oct 26 18:00:11 2024

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