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Manganese 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:

Mercury (Hg) 5 atoms
Chlorine (Cl) 1 atom

Manganese Binding Sites:

The binding sites of Manganese 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 Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Lactose, PDB code: 1zi1:

Manganese binding site 1 out of 1 in 1zi1

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn 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:Mn450

b:58.7
occ:0.50
 OD1 A:ASP211 2.9 32.0 1.0
CE A:MET214 2.9 28.8 1.0
OD1 A:ASP213 3.0 25.8 1.0
OD2 A:ASP213 3.3 28.4 1.0
CG A:ASP213 3.5 26.6 1.0
CG A:ASP211 3.6 27.4 1.0
CB A:ASP211 3.6 26.2 1.0
O A:HOH700 3.9 40.6 1.0
SD A:MET214 4.6 26.8 1.0
OD2 A:ASP211 4.7 29.3 1.0
O A:ASP213 4.8 22.2 1.0
CG A:MET214 5.0 23.4 1.0
O A:HOH673 5.0 47.6 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: Sat Oct 5 13:17:13 2024

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