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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

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