Atomistry » Manganese » PDB 1g15-1hkd » 1g8o
Atomistry »
  Manganese »
    PDB 1g15-1hkd »
      1g8o »

Manganese in PDB 1g8o: Crystallographic Structure of the Native Bovine Alpha-1,3- Galactosyltransferase Catalytic Domain

Enzymatic activity of Crystallographic Structure of the Native Bovine Alpha-1,3- Galactosyltransferase Catalytic Domain

All present enzymatic activity of Crystallographic Structure of the Native Bovine Alpha-1,3- Galactosyltransferase Catalytic Domain:
2.4.1.151;

Protein crystallography data

The structure of Crystallographic Structure of the Native Bovine Alpha-1,3- Galactosyltransferase Catalytic Domain, PDB code: 1g8o was solved by L.N.Gastinel, C.Bigon, A.K.Misra, O.Hindsgaul, J.H.Shaper, D.H.Joziasse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 2.44 / 2.30
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 95.558, 95.558, 112.711, 90.00, 90.00, 90.00
R / Rfree (%) 27.4 / 33.5

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystallographic Structure of the Native Bovine Alpha-1,3- Galactosyltransferase Catalytic Domain (pdb code 1g8o). 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 Crystallographic Structure of the Native Bovine Alpha-1,3- Galactosyltransferase Catalytic Domain, PDB code: 1g8o:

Manganese binding site 1 out of 1 in 1g8o

Go back to Manganese Binding Sites List in 1g8o
Manganese binding site 1 out of 1 in the Crystallographic Structure of the Native Bovine Alpha-1,3- Galactosyltransferase Catalytic Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystallographic Structure of the Native Bovine Alpha-1,3- Galactosyltransferase Catalytic Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn475

b:45.6
occ:0.50
 O A:HOH573 2.3 55.7 1.0
OD2 A:ASP225 2.5 50.9 1.0
OD1 A:ASP227 2.5 55.9 1.0
OD2 A:ASP227 2.8 58.1 1.0
O2P A:U5P474 2.8 51.2 0.5
CG A:ASP227 3.0 54.4 1.0
O5' A:U5P474 3.1 48.4 0.5
ND2 A:ASN362 3.3 90.0 1.0
CG A:ASP225 3.4 45.6 1.0
P A:U5P474 3.6 48.7 0.5
CB A:ASP225 3.7 44.5 1.0
O3' A:U5P474 3.7 39.3 0.5
CG A:ASN362 4.1 90.0 1.0
OD1 A:ASN362 4.2 90.0 1.0
O3P A:U5P474 4.3 48.7 0.5
C5' A:U5P474 4.4 43.2 0.5
CB A:LYS359 4.4 83.0 1.0
OD1 A:ASP225 4.5 47.8 1.0
O A:HOH543 4.5 82.0 1.0
CB A:ASP227 4.5 51.0 1.0
C3' A:U5P474 4.6 39.9 0.5
O A:HOH542 4.6 60.5 1.0
O A:ASP227 4.7 45.3 1.0
O1P A:U5P474 4.7 49.0 0.5
CA A:LYS359 4.8 90.0 1.0
N A:GLU360 4.9 90.0 1.0
C4' A:U5P474 4.9 41.8 0.5

Reference:

L.N.Gastinel, C.Bignon, A.K.Misra, O.Hindsgaul, J.H.Shaper, D.H.Joziasse. Bovine ALPHA1,3-Galactosyltransferase Catalytic Domain Structure and Its Relationship with Abo Histo-Blood Group and Glycosphingolipid Glycosyltransferases. Embo J. V. 20 638 2001.
ISSN: ISSN 0261-4189
PubMed: 11179209
DOI: 10.1093/EMBOJ/20.4.638
Page generated: Sat Oct 5 10:31:31 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy