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Mercury in PDB 1fo8: Crystal Structure of N-Acetylglucosaminyltransferase I

Enzymatic activity of Crystal Structure of N-Acetylglucosaminyltransferase I

All present enzymatic activity of Crystal Structure of N-Acetylglucosaminyltransferase I:
2.4.1.101;

Protein crystallography data

The structure of Crystal Structure of N-Acetylglucosaminyltransferase I, PDB code: 1fo8 was solved by U.M.Unligil, S.Zhou, S.Yuwaraj, M.Sarkar, H.Schachter, J.M.Rini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.72 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.382, 82.378, 102.487, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 18.5

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of N-Acetylglucosaminyltransferase I (pdb code 1fo8). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Crystal Structure of N-Acetylglucosaminyltransferase I, PDB code: 1fo8:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in 1fo8

Go back to Mercury Binding Sites List in 1fo8
Mercury binding site 1 out of 2 in the Crystal Structure of N-Acetylglucosaminyltransferase I


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of N-Acetylglucosaminyltransferase I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1448

b:10.1
occ:0.90
HG A:MMC1448 0.0 10.1 0.9
C A:MMC1448 2.0 10.2 0.9
SG A:CYS123 2.3 12.4 0.9
O A:LEU214 3.0 10.0 1.0
CB A:CYS123 3.1 7.3 0.1
CB A:CYS123 3.3 7.2 0.9
O A:HOH1520 3.4 12.6 1.0
O A:GLU211 3.6 10.9 1.0
CD1 A:LEU127 3.7 7.8 1.0
CG2 A:VAL210 3.8 10.4 1.0
CA A:CYS123 3.8 8.7 0.9
CA A:CYS123 3.8 7.7 0.1
C A:LEU214 3.9 8.8 1.0
O A:CYS123 4.0 8.2 0.9
O A:CYS123 4.0 7.4 0.1
C A:CYS123 4.1 7.6 0.9
C A:CYS123 4.1 7.5 0.1
CG A:LEU127 4.1 6.8 1.0
CB A:VAL210 4.1 9.6 1.0
CB A:LEU214 4.2 9.0 1.0
CA A:LEU214 4.4 7.6 1.0
N A:LEU214 4.5 8.2 1.0
SG A:CYS123 4.5 8.8 0.1
C A:GLU211 4.6 11.7 1.0
CD2 A:LEU127 4.8 6.7 1.0
CG1 A:VAL216 4.9 8.7 1.0
HG A:MMC1448 4.9 16.0 0.1
CG1 A:VAL210 4.9 14.4 1.0
N A:GLU215 4.9 8.3 1.0
CG2 A:VAL112 5.0 8.8 1.0
N A:LEU124 5.0 7.7 1.0

Mercury binding site 2 out of 2 in 1fo8

Go back to Mercury Binding Sites List in 1fo8
Mercury binding site 2 out of 2 in the Crystal Structure of N-Acetylglucosaminyltransferase I


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structure of N-Acetylglucosaminyltransferase I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1448

b:16.0
occ:0.10
HG A:MMC1448 0.0 16.0 0.1
CZ A:PHE316 1.7 13.1 0.9
CE2 A:PHE316 1.7 13.0 0.9
C A:MMC1448 2.0 16.2 0.1
SG A:CYS123 2.3 8.8 0.1
CE1 A:PHE316 2.9 12.9 0.1
O A:ASP212 2.9 14.7 1.0
CB A:CYS123 3.0 7.2 0.9
CE1 A:PHE316 3.0 13.1 0.9
CD2 A:PHE316 3.0 12.5 0.9
CB A:CYS123 3.0 7.3 0.1
O A:LEU214 3.0 10.0 1.0
N A:LEU214 3.2 8.2 1.0
C A:ASP213 3.3 9.9 1.0
CA A:CYS123 3.3 8.7 0.9
N A:CYS123 3.3 8.6 0.9
N A:CYS123 3.3 8.2 0.1
CA A:CYS123 3.3 7.7 0.1
CD1 A:PHE316 3.3 14.1 0.1
CA A:ASP213 3.4 12.2 1.0
CZ A:PHE316 3.5 13.5 0.1
C A:LEU214 3.5 8.8 1.0
C A:ASP212 3.6 13.1 1.0
N A:ASP213 3.9 11.0 1.0
CA A:LEU214 3.9 7.6 1.0
CD1 A:PHE316 3.9 13.7 0.9
CG A:PHE316 3.9 14.0 0.9
O A:ASP213 4.0 10.4 1.0
O A:THR119 4.1 14.6 1.0
C A:ARG122 4.2 8.7 1.0
CG A:PHE316 4.2 14.1 0.1
N A:GLU215 4.3 8.3 1.0
CE2 A:PHE316 4.3 13.2 0.1
CB A:ARG122 4.4 11.2 1.0
SG A:CYS123 4.5 12.4 0.9
O A:HOH1674 4.6 20.2 1.0
CG A:ARG122 4.6 15.2 1.0
CD2 A:PHE316 4.6 13.7 0.1
CA A:ASP212 4.7 13.1 1.0
CA A:ARG122 4.8 8.6 1.0
CB A:ASP213 4.8 14.6 1.0
CA A:GLU215 4.8 9.6 1.0
C A:CYS123 4.8 7.6 0.9
O A:ARG122 4.8 9.8 1.0
C A:CYS123 4.9 7.5 0.1
HG A:MMC1448 4.9 10.1 0.9
CD A:ARG122 5.0 17.8 1.0

Reference:

U.M.Unligil, S.Zhou, S.Yuwaraj, M.Sarkar, H.Schachter, J.M.Rini. X-Ray Crystal Structure of Rabbit N-Acetylglucosaminyltransferase I: Catalytic Mechanism and A New Protein Superfamily. Embo J. V. 19 5269 2000.
ISSN: ISSN 0261-4189
PubMed: 11032794
DOI: 10.1093/EMBOJ/19.20.5269
Page generated: Sun Dec 13 19:02:41 2020

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