Mercury in PDB 1wsz: Mutant Human Abo(H) Blood Group Transferase A

All present enzymatic activity of Mutant Human Abo(H) Blood Group Transferase A:
2.4.1.40;

The structure of Mutant Human Abo(H) Blood Group Transferase A, PDB code: 1wsz was solved by H.J.Lee, C.H.Barry, S.N.Borisova, N.O.L.Seto, R.B.Zheng, A.Blancher, S.V.Evans, M.M.Palcic, 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, 150.100, 79.700, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 24.4

The binding sites of Mercury atom in the Mutant Human Abo(H) Blood Group Transferase A (pdb code 1wsz). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 4 binding sites of Mercury where determined in the Mutant Human Abo(H) Blood Group Transferase A, PDB code: 1wsz:
Jump to Mercury binding site number: 1; 2; 3; 4;

Mercury binding site 1 out of 4 in the Mutant Human Abo(H) Blood Group Transferase A


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Mutant Human Abo(H) Blood Group Transferase A within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg401 b:43.4 occ:0.50 SD A:MET288 2.9 37.6 1.0 OD1 A:ASP302 2.9 40.8 1.0 O A:CYS284 3.6 33.3 1.0 C A:CYS284 3.7 32.0 1.0 CB A:CYS284 3.9 32.3 1.0 CG A:MET288 3.9 32.9 1.0 N A:HIS285 3.9 32.8 1.0 CA A:HIS285 4.0 34.5 1.0 CG A:ASP302 4.1 39.0 1.0 CA A:CYS284 4.4 31.4 1.0 CE A:MET288 4.6 38.4 1.0 CB A:MET288 4.6 31.4 1.0 CB A:HIS285 4.7 36.8 1.0 CB A:ASP302 4.8 34.8 1.0 HG A:HG402 4.8 47.2 0.5 O A:THR281 4.9 26.5 1.0

Mercury binding site 2 out of 4 in the Mutant Human Abo(H) Blood Group Transferase A


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Mutant Human Abo(H) Blood Group Transferase A within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg402 b:47.2 occ:0.50 SG A:CYS284 2.6 36.9 1.0 CB A:CYS284 3.1 32.3 1.0 CD2 A:LEU280 3.3 23.9 1.0 CB A:LEU306 3.7 22.1 1.0 O A:ASP302 3.7 26.3 1.0 CA A:LEU306 3.8 20.3 1.0 N A:LEU306 3.9 20.8 1.0 O A:HOH667 4.2 41.4 1.0 CG A:LEU306 4.4 23.7 1.0 CD1 A:LEU306 4.4 26.8 1.0 C A:HIS305 4.5 22.6 1.0 CG A:LEU280 4.6 22.1 1.0 C A:ASP302 4.6 28.4 1.0 CA A:CYS284 4.6 31.4 1.0 O A:LEU280 4.6 22.2 1.0 CB A:HIS305 4.8 25.8 1.0 HG A:HG401 4.8 43.4 0.5 CB A:ASP302 4.9 34.8 1.0 CA A:ASP302 4.9 31.0 1.0 O A:HIS305 5.0 21.0 1.0

Mercury binding site 3 out of 4 in the Mutant Human Abo(H) Blood Group Transferase A


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Mutant Human Abo(H) Blood Group Transferase A within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg403 b:40.6 occ:1.00 SG A:CYS209 2.5 29.0 1.0 OG1 A:THR119 2.9 23.1 1.0 CB A:CYS209 3.2 21.4 1.0 O A:HOH501 3.9 18.6 1.0 CB A:THR119 3.9 21.9 1.0 CG2 A:THR119 4.1 22.4 1.0 CA A:CYS209 4.2 20.1 1.0 CG1 A:VAL277 4.4 20.2 1.0 N A:CYS209 4.7 18.2 1.0 CD1 A:LEU207 4.8 24.5 1.0 CZ A:PHE270 4.8 21.3 1.0

Mercury binding site 4 out of 4 in the Mutant Human Abo(H) Blood Group Transferase A


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Mutant Human Abo(H) Blood Group Transferase A within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg404 b:41.5 occ:0.50 SG A:CYS284 2.6 36.9 1.0 O A:HIS305 3.1 21.0 1.0 CA A:CYS284 3.3 31.4 1.0 N A:CYS284 3.5 29.2 1.0 CB A:CYS284 3.5 32.3 1.0 CB A:TYR309 3.6 19.4 1.0 C A:HIS305 3.8 22.6 1.0 C A:ALA283 3.9 28.5 1.0 CB A:HIS305 3.9 25.8 1.0 O A:ALA283 4.1 29.7 1.0 CD1 A:TYR309 4.1 18.7 1.0 CG A:TYR309 4.2 17.1 1.0 CA A:HIS305 4.3 23.3 1.0 CB A:ALA283 4.3 26.9 1.0 N A:TYR309 4.3 18.4 1.0 CA A:TYR309 4.3 19.1 1.0 O A:LEU280 4.6 22.2 1.0 CB A:ALA287 4.6 29.1 1.0 N A:LEU306 4.7 20.8 1.0 C A:CYS284 4.7 32.0 1.0 CA A:ALA283 4.8 28.0 1.0 CG A:HIS305 4.8 26.3 1.0 O A:HOH606 4.8 36.2 1.0 CD2 A:HIS305 4.9 26.3 1.0 CA A:LEU306 5.0 20.3 1.0

H.J.Lee, C.H.Barry, S.N.Borisova, N.O.L.Seto, R.B.Zheng, A.Blancher, S.V.Evans, M.M.Palcic. Structural Basis For the Inactivity of Human Blood Group O2 Glycosyltransferase J.Biol.Chem. V. 280 525 2005.
ISSN: ISSN 0021-9258
PubMed: 15475562
DOI: 10.1074/JBC.M410245200