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Mercury in PDB 1zi1: Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Lactose

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

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

Protein crystallography data

The structure of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Lactose, PDB code: 1zi1 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 / 1.57
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.600, 149.400, 79.600, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 22.8

Other elements in 1zi1:

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

Manganese (Mn) 1 atom
Chlorine (Cl) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Lactose (pdb code 1zi1). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 5 binding sites of Mercury where determined in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Lactose, PDB code: 1zi1:
Jump to Mercury binding site number: 1; 2; 3; 4; 5;

Mercury binding site 1 out of 5 in 1zi1

Go back to Mercury Binding Sites List in 1zi1
Mercury binding site 1 out of 5 in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Lactose


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 Lactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg401

b:28.6
occ:0.30
 SG A:CYS284 2.5 33.8 1.0
CB A:CYS284 3.1 28.9 1.0
CD2 A:LEU280 3.5 20.8 1.0
O A:ASP302 3.7 26.4 1.0
CA A:LEU306 3.7 19.9 1.0
N A:LEU306 3.7 19.2 1.0
CB A:LEU306 3.8 20.4 1.0
CD1 A:LEU306 4.3 23.5 1.0
C A:HIS305 4.3 21.1 1.0
CB A:HIS305 4.5 24.4 1.0
O A:LEU280 4.6 21.4 1.0
CA A:CYS284 4.6 27.2 1.0
C A:ASP302 4.6 27.4 1.0
CG A:LEU280 4.6 18.2 1.0
CG A:LEU306 4.7 21.5 1.0
O A:HIS305 4.8 20.7 1.0
HG A:HG402 4.9 27.0 0.3
CB A:ASP302 4.9 33.5 1.0
HG A:HG405 4.9 34.6 0.3
CA A:ASP302 4.9 30.0 1.0

Mercury binding site 2 out of 5 in 1zi1

Go back to Mercury Binding Sites List in 1zi1
Mercury binding site 2 out of 5 in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Lactose


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 Lactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg402

b:27.0
occ:0.30
 SG A:CYS284 2.5 33.8 1.0
O A:HIS305 3.1 20.7 1.0
CA A:CYS284 3.3 27.2 1.0
N A:CYS284 3.4 26.1 1.0
CB A:CYS284 3.5 28.9 1.0
CB A:TYR309 3.6 18.1 1.0
C A:HIS305 3.8 21.1 1.0
C A:ALA283 3.8 26.1 1.0
CB A:HIS305 3.9 24.4 1.0
CD1 A:TYR309 4.0 17.7 1.0
O A:ALA283 4.1 26.3 1.0
CG A:TYR309 4.2 17.6 1.0
CB A:ALA283 4.2 23.3 1.0
CA A:HIS305 4.3 21.9 1.0
N A:TYR309 4.3 18.1 1.0
CA A:TYR309 4.3 18.6 1.0
O A:LEU280 4.6 21.4 1.0
CB A:ALA287 4.7 29.6 1.0
C A:CYS284 4.7 27.5 1.0
CA A:ALA283 4.7 25.6 1.0
N A:LEU306 4.7 19.2 1.0
CG A:HIS305 4.8 26.9 1.0
CD2 A:HIS305 4.9 26.7 1.0
HG A:HG401 4.9 28.6 0.3

Mercury binding site 3 out of 5 in 1zi1

Go back to Mercury Binding Sites List in 1zi1
Mercury binding site 3 out of 5 in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Lactose


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 Lactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg403

b:29.6
occ:0.70
 O A:GLY98 2.6 23.9 1.0
SG A:CYS80 2.6 37.7 1.0
O A:HOH621 3.2 42.7 1.0
CB A:CYS80 3.3 35.3 1.0
CA A:CYS80 3.3 32.9 1.0
C A:GLY98 3.7 21.9 1.0
O A:CYS80 3.9 32.8 1.0
C A:CYS80 4.0 33.2 1.0
O A:HOH589 4.1 33.1 1.0
CA A:THR99 4.3 19.3 1.0
O A:HOH546 4.4 28.8 1.0
N A:THR99 4.4 19.5 1.0
N A:CYS80 4.6 32.7 1.0
CA A:GLY98 4.7 21.3 1.0
C A:THR99 4.9 19.6 1.0
O A:THR99 5.0 20.1 1.0

Mercury binding site 4 out of 5 in 1zi1

Go back to Mercury Binding Sites List in 1zi1
Mercury binding site 4 out of 5 in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Lactose


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 Lactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg404

b:28.7
occ:0.70
 SG A:CYS209 2.4 26.5 1.0
OG1 A:THR119 2.8 24.9 1.0
CB A:CYS209 3.3 21.1 1.0
CL A:CL406 3.8 30.8 1.0
CB A:THR119 3.9 21.0 1.0
CG2 A:THR119 4.0 23.2 1.0
CA A:CYS209 4.2 19.1 1.0
CG1 A:VAL277 4.3 16.4 1.0
N A:CYS209 4.7 17.9 1.0
CZ A:PHE270 4.9 21.6 1.0
CD1 A:LEU207 4.9 23.3 1.0

Mercury binding site 5 out of 5 in 1zi1

Go back to Mercury Binding Sites List in 1zi1
Mercury binding site 5 out of 5 in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Lactose


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 5 of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Lactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg405

b:34.6
occ:0.30
 SD A:MET288 2.8 40.2 1.0
OD2 A:ASP302 3.3 39.5 1.0
C A:CYS284 3.7 27.5 1.0
N A:HIS285 3.7 27.1 1.0
O A:CYS284 3.8 28.1 1.0
CB A:CYS284 3.8 28.9 1.0
CG A:MET288 3.8 34.9 1.0
CA A:HIS285 3.9 30.1 1.0
CG A:ASP302 4.2 36.8 1.0
CA A:CYS284 4.4 27.2 1.0
CE A:MET288 4.5 40.0 1.0
CB A:MET288 4.6 32.1 1.0
CB A:HIS285 4.6 32.3 1.0
CB A:ASP302 4.8 33.5 1.0
O A:THR281 4.9 24.7 1.0
HG A:HG401 4.9 28.6 0.3
OD1 A:ASP302 4.9 40.5 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 02:09:42 2024

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