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Mercury in PDB 1zi3: Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine

Enzymatic activity of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine

All present enzymatic activity of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine:
2.4.1.40;

Protein crystallography data

The structure of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine, PDB code: 1zi3 was solved by J.A.Letts, N.L.Rose, Y.R.Fang, C.H.Barry, S.N.Borisova, N.O.Seto, M.M.Palcic, S.V.Evans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.69
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.490, 149.210, 79.320, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 23.4

Other elements in 1zi3:

The structure of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine (pdb code 1zi3). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 4 binding sites of Mercury where determined in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine, PDB code: 1zi3:
Jump to Mercury binding site number: 1; 2; 3; 4;

Mercury binding site 1 out of 4 in 1zi3

Go back to Mercury Binding Sites List in 1zi3
Mercury binding site 1 out of 4 in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine


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 Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg401

b:36.5
occ:0.39
 O A:HOH698 2.4 43.3 1.0
O A:HOH647 2.6 39.7 1.0
SG A:CYS284 2.9 35.3 1.0
CB A:CYS284 3.0 28.4 1.0
CD2 A:LEU280 3.3 20.2 1.0
CA A:LEU306 3.9 20.1 1.0
O A:ASP302 3.9 24.7 1.0
N A:LEU306 4.0 19.3 1.0
CB A:LEU306 4.0 19.3 1.0
CD1 A:LEU306 4.3 24.5 1.0
O A:LEU280 4.4 20.7 1.0
CG A:LEU280 4.4 18.4 1.0
CA A:CYS284 4.4 26.7 1.0
C A:HIS305 4.5 21.0 1.0
CB A:HIS305 4.8 22.8 1.0
CG A:LEU306 4.8 22.5 1.0
C A:ASP302 4.9 25.8 1.0
HG A:HG402 4.9 39.3 0.4
O A:HIS305 4.9 20.1 1.0
C A:LEU280 5.0 20.7 1.0
O A:HOH506 5.0 20.6 1.0

Mercury binding site 2 out of 4 in 1zi3

Go back to Mercury Binding Sites List in 1zi3
Mercury binding site 2 out of 4 in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine


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 Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg402

b:39.3
occ:0.39
 SG A:CYS284 2.7 35.3 1.0
SD A:MET288 2.8 41.0 1.0
OD2 A:ASP302 3.3 38.2 1.0
O A:HOH698 3.3 43.3 1.0
CB A:CYS284 3.6 28.4 1.0
C A:CYS284 3.7 27.6 1.0
N A:HIS285 3.7 28.2 1.0
CG A:MET288 3.9 35.7 1.0
O A:CYS284 3.9 28.1 1.0
CA A:HIS285 3.9 30.3 1.0
CG A:ASP302 4.1 35.5 1.0
CA A:CYS284 4.3 26.7 1.0
CE A:MET288 4.5 40.2 1.0
CB A:MET288 4.6 32.2 1.0
CB A:HIS285 4.7 33.1 1.0
CB A:ASP302 4.8 31.3 1.0
OD1 A:ASP302 4.8 37.6 1.0
O A:THR281 4.9 24.6 1.0
HG A:HG401 4.9 36.5 0.4

Mercury binding site 3 out of 4 in 1zi3

Go back to Mercury Binding Sites List in 1zi3
Mercury binding site 3 out of 4 in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg403

b:27.9
occ:0.60
 SG A:CYS209 2.4 26.6 1.0
O A:HOH699 2.5 36.6 1.0
OG1 A:THR119 2.9 23.7 1.0
CB A:CYS209 3.3 21.7 1.0
CB A:THR119 3.9 20.4 1.0
CG2 A:THR119 4.0 22.6 1.0
O A:HOH648 4.0 24.9 1.0
CA A:CYS209 4.2 18.6 1.0
CG1 A:VAL277 4.3 16.4 1.0
N A:CYS209 4.7 18.4 1.0
CD1 A:LEU207 4.7 24.4 1.0
CZ A:PHE270 4.9 19.9 1.0
CB A:LEU207 5.0 20.4 1.0
CE1 A:PHE270 5.0 20.9 1.0

Mercury binding site 4 out of 4 in 1zi3

Go back to Mercury Binding Sites List in 1zi3
Mercury binding site 4 out of 4 in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with N-Acetyllactosamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg405

b:33.4
occ:0.45
 SG A:CYS80 2.7 48.1 1.0
O A:GLY98 2.7 22.8 1.0
CB A:CYS80 3.0 42.7 1.0
CA A:CYS80 3.1 40.0 1.0
O A:CYS80 3.8 38.8 1.0
C A:CYS80 3.8 38.8 1.0
C A:GLY98 3.9 22.3 1.0
O A:HOH693 4.1 37.6 1.0
O A:HOH689 4.2 52.7 1.0
N A:CYS80 4.3 39.9 1.0
CA A:THR99 4.3 19.8 1.0
O A:HOH581 4.5 44.1 1.0
N A:THR99 4.5 19.3 1.0
C A:THR99 4.9 19.7 1.0
CA A:GLY98 4.9 21.6 1.0
N A:ARG81 5.0 36.7 1.0

Reference:

J.A.Letts, N.L.Rose, Y.R.Fang, C.H.Barry, S.N.Borisova, N.O.Seto, M.M.Palcic, S.V.Evans. Differential Recognition of the Type I and II H Antigen Acceptors By the Human Abo(H) Blood Group A and B Glycosyltransferases. J.Biol.Chem. V. 281 3625 2006.
ISSN: ISSN 0021-9258
PubMed: 16326711
DOI: 10.1074/JBC.M507620200
Page generated: Sun Aug 11 02:09:47 2024

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