Atomistry » Mercury » PDB 1yu1-2epm » 1zhj
Atomistry »
  Mercury »
    PDB 1yu1-2epm »
      1zhj »

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

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

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

Protein crystallography data

The structure of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Galactose, PDB code: 1zhj 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 / 1.59
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.700, 149.500, 79.600, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 22

Other elements in 1zhj:

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

Chlorine (Cl) 2 atoms

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Galactose (pdb code 1zhj). 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 Galactose, PDB code: 1zhj:
Jump to Mercury binding site number: 1; 2; 3; 4; 5;

Mercury binding site 1 out of 5 in 1zhj

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


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

b:30.4
occ:0.35
 SG A:CYS284 2.5 34.2 1.0
CB A:CYS284 3.1 27.6 1.0
CD2 A:LEU280 3.4 18.4 1.0
CB A:LEU306 3.7 19.3 1.0
O A:ASP302 3.7 22.6 1.0
CA A:LEU306 3.8 17.4 1.0
N A:LEU306 3.8 16.5 1.0
CD1 A:LEU306 4.4 25.0 1.0
C A:HIS305 4.4 17.6 1.0
CG A:LEU306 4.5 21.5 1.0
CG A:LEU280 4.5 17.7 1.0
O A:LEU280 4.5 18.5 1.0
CA A:CYS284 4.6 26.6 1.0
C A:ASP302 4.6 23.7 1.0
CB A:HIS305 4.7 20.0 1.0
CB A:ASP302 4.9 29.4 1.0
O A:HIS305 4.9 17.2 1.0
CA A:ASP302 5.0 25.8 1.0
HG A:HG407 5.0 25.2 0.2
HG A:HG402 5.0 33.6 0.5

Mercury binding site 2 out of 5 in 1zhj

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


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

b:33.6
occ:0.50
 SD A:MET288 3.0 37.9 1.0
OD2 A:ASP302 3.2 36.2 1.0
C A:CYS284 3.7 26.5 1.0
O A:CYS284 3.7 27.9 1.0
N A:HIS285 3.7 27.2 1.0
CB A:CYS284 3.8 27.6 1.0
CG A:MET288 3.8 33.5 1.0
CA A:HIS285 3.9 29.7 1.0
CG A:ASP302 4.1 32.4 1.0
CA A:CYS284 4.4 26.6 1.0
CB A:MET288 4.5 30.7 1.0
CB A:HIS285 4.6 32.2 1.0
CE A:MET288 4.7 37.5 1.0
OD1 A:ASP302 4.7 36.7 1.0
CB A:ASP302 4.8 29.4 1.0
O A:THR281 4.8 22.7 1.0
HG A:HG401 5.0 30.4 0.3

Mercury binding site 3 out of 5 in 1zhj

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


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

b:25.8
occ:0.70
 SG A:CYS209 2.4 23.8 1.0
OG1 A:THR119 2.9 22.5 1.0
CB A:CYS209 3.3 16.5 1.0
CL A:CL403 3.7 34.4 1.0
CB A:THR119 3.9 18.2 1.0
CG2 A:THR119 3.9 19.3 1.0
CA A:CYS209 4.2 16.0 1.0
CG1 A:VAL277 4.3 16.8 1.0
N A:CYS209 4.7 15.2 1.0
CD1 A:LEU207 4.8 22.7 1.0
CZ A:PHE270 4.9 20.1 1.0

Mercury binding site 4 out of 5 in 1zhj

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


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 Galactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg405

b:32.7
occ:0.40
 O A:GLY98 2.7 20.8 1.0
SG A:CYS80 2.7 46.6 1.0
CB A:CYS80 2.9 39.9 1.0
CA A:CYS80 3.0 37.5 1.0
O A:HOH668 3.7 33.7 1.0
C A:CYS80 3.8 36.1 1.0
C A:GLY98 3.8 19.5 1.0
O A:CYS80 3.9 37.0 1.0
O A:HOH649 4.2 43.8 1.0
N A:CYS80 4.2 36.5 1.0
CA A:THR99 4.3 16.6 1.0
N A:THR99 4.5 17.1 1.0
CA A:GLY98 4.8 19.2 1.0
N A:ARG81 4.8 34.6 1.0
C A:THR99 4.9 16.5 1.0

Mercury binding site 5 out of 5 in 1zhj

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


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 Galactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg407

b:25.2
occ:0.20
 SG A:CYS284 2.7 34.2 1.0
O A:HOH736 2.7 42.5 1.0
O A:HIS305 3.1 17.2 1.0
CA A:CYS284 3.4 26.6 1.0
O A:HOH737 3.4 24.5 1.0
N A:CYS284 3.5 24.2 1.0
CB A:TYR309 3.6 15.2 1.0
CB A:CYS284 3.6 27.6 1.0
C A:HIS305 3.7 17.6 1.0
CB A:HIS305 3.8 20.0 1.0
C A:ALA283 3.9 24.1 1.0
O A:ALA283 4.0 24.9 1.0
CD1 A:TYR309 4.1 15.6 1.0
CA A:HIS305 4.2 18.2 1.0
CB A:ALA283 4.2 21.0 1.0
CG A:TYR309 4.3 14.4 1.0
N A:TYR309 4.3 16.3 1.0
CA A:TYR309 4.3 16.1 1.0
CB A:ALA287 4.5 27.0 1.0
N A:LEU306 4.6 16.5 1.0
O A:LEU280 4.7 18.5 1.0
CG A:HIS305 4.7 22.0 1.0
CA A:ALA283 4.7 23.3 1.0
C A:CYS284 4.8 26.5 1.0
CD2 A:HIS305 4.9 21.1 1.0
HG A:HG401 5.0 30.4 0.3
CA A:LEU306 5.0 17.4 1.0
O A:HOH729 5.0 41.6 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 02:07:45 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy