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Mercury in PDB 2o1f: Natural Occuring Mutation of Human Abo(H) Galactosyltransferase: Gtb/M214R

Protein crystallography data

The structure of Natural Occuring Mutation of Human Abo(H) Galactosyltransferase: Gtb/M214R, PDB code: 2o1f was solved by J.A.Letts, S.N.Borisova, S.V.Evans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.99
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.520, 149.670, 79.740, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 23.6

Mercury Binding Sites:

The binding sites of Mercury atom in the Natural Occuring Mutation of Human Abo(H) Galactosyltransferase: Gtb/M214R (pdb code 2o1f). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Natural Occuring Mutation of Human Abo(H) Galactosyltransferase: Gtb/M214R, PDB code: 2o1f:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in 2o1f

Go back to Mercury Binding Sites List in 2o1f
Mercury binding site 1 out of 3 in the Natural Occuring Mutation of Human Abo(H) Galactosyltransferase: Gtb/M214R


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Natural Occuring Mutation of Human Abo(H) Galactosyltransferase: Gtb/M214R within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg401

b:44.0
occ:0.50
SG A:CYS284 2.5 26.0 0.5
OD1 A:ASP302 2.9 42.0 1.0
SD A:MET288 3.1 39.5 1.0
O A:CYS284 3.5 29.7 0.5
CB A:CYS284 3.5 26.8 0.5
C A:CYS284 3.5 29.8 0.5
N A:HIS285 3.7 29.9 1.0
C A:CYS284 3.8 28.9 0.5
CG A:ASP302 3.9 38.7 1.0
CB A:CYS284 3.9 29.0 0.5
CA A:HIS285 4.0 32.4 1.0
CG A:MET288 4.0 35.9 1.0
O A:CYS284 4.1 28.9 0.5
CA A:CYS284 4.3 27.7 0.5
CA A:CYS284 4.3 29.2 0.5
CB A:ASP302 4.5 32.9 1.0
CB A:MET288 4.6 33.6 1.0
CB A:HIS285 4.6 33.4 1.0
OD2 A:ASP302 4.7 43.6 1.0
CE A:MET288 4.8 43.4 1.0
HG A:HG402 4.8 43.7 0.5
O A:THR281 4.9 28.0 1.0
CA A:ASP302 5.0 31.3 1.0

Mercury binding site 2 out of 3 in 2o1f

Go back to Mercury Binding Sites List in 2o1f
Mercury binding site 2 out of 3 in the Natural Occuring Mutation of Human Abo(H) Galactosyltransferase: Gtb/M214R


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Natural Occuring Mutation of Human Abo(H) Galactosyltransferase: Gtb/M214R within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg402

b:43.7
occ:0.50
SG A:CYS284 2.7 32.0 0.5
CB A:CYS284 2.9 29.0 0.5
SG A:CYS284 3.0 26.0 0.5
CB A:CYS284 3.1 26.8 0.5
CD2 A:LEU280 3.6 24.2 1.0
O A:ASP302 3.8 27.5 1.0
CA A:LEU306 4.0 22.1 1.0
N A:LEU306 4.0 22.4 1.0
CB A:LEU306 4.1 21.3 1.0
CA A:CYS284 4.4 27.7 0.5
CD1 A:LEU306 4.5 23.5 1.0
CA A:CYS284 4.5 29.2 0.5
CG A:LEU280 4.5 24.2 1.0
O A:LEU280 4.6 24.9 1.0
C A:HIS305 4.6 23.8 1.0
C A:ASP302 4.7 28.9 1.0
CB A:ASP302 4.7 32.9 1.0
CB A:HIS305 4.8 24.8 1.0
HG A:HG401 4.8 44.0 0.5
CG A:LEU306 5.0 20.8 1.0
CA A:ASP302 5.0 31.3 1.0

Mercury binding site 3 out of 3 in 2o1f

Go back to Mercury Binding Sites List in 2o1f
Mercury binding site 3 out of 3 in the Natural Occuring Mutation of Human Abo(H) Galactosyltransferase: Gtb/M214R


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Natural Occuring Mutation of Human Abo(H) Galactosyltransferase: Gtb/M214R within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg403

b:30.6
occ:0.70
O A:HOH524 1.3 14.8 1.0
SG A:CYS209 2.4 28.4 1.0
OG1 A:THR119 2.9 28.1 1.0
CB A:CYS209 3.2 23.1 1.0
CB A:THR119 3.9 25.6 1.0
CG2 A:THR119 3.9 24.8 1.0
O A:HOH422 4.0 30.1 1.0
CG1 A:VAL277 4.1 19.8 1.0
CA A:CYS209 4.1 23.1 1.0
CD1 A:LEU207 4.6 25.3 1.0
N A:CYS209 4.8 21.5 1.0
CD2 A:LEU207 4.9 27.1 1.0
CZ A:PHE270 4.9 23.4 1.0
CB A:LEU207 5.0 23.6 1.0

Reference:

M.Persson, J.A.Letts, B.Hosseini-Maaf, S.N.Borisova, M.M.Palcic, S.V.Evans, M.L.Olsson. Structural Effects of Naturally Occurring Human Blood Group B Galactosyltransferase Mutations Adjacent to the Dxd Motif. J.Biol.Chem. V. 282 9564 2007.
ISSN: ISSN 0021-9258
PubMed: 17259183
DOI: 10.1074/JBC.M610998200
Page generated: Sun Dec 13 19:07:29 2020

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