Atomistry » Calcium » PDB 1yf4-1yvn » 1yro
Atomistry »
  Calcium »
    PDB 1yf4-1yvn »
      1yro »

Calcium in PDB 1yro: Crystal Structure of BETA14,-Galactosyltransferase Mutant ARG228LYS in Complex with Alpha-Lactalbumin in the Presence of Udp-Galactose and Mn

Enzymatic activity of Crystal Structure of BETA14,-Galactosyltransferase Mutant ARG228LYS in Complex with Alpha-Lactalbumin in the Presence of Udp-Galactose and Mn

All present enzymatic activity of Crystal Structure of BETA14,-Galactosyltransferase Mutant ARG228LYS in Complex with Alpha-Lactalbumin in the Presence of Udp-Galactose and Mn:
2.4.1.22; 2.4.1.38; 2.4.1.90;

Protein crystallography data

The structure of Crystal Structure of BETA14,-Galactosyltransferase Mutant ARG228LYS in Complex with Alpha-Lactalbumin in the Presence of Udp-Galactose and Mn, PDB code: 1yro was solved by B.Ramakrishnan, E.Boeggeman, P.K.Qasba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.55 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 57.334, 94.087, 99.705, 90.00, 101.64, 90.00
R / Rfree (%) 18.9 / 22.5

Other elements in 1yro:

The structure of Crystal Structure of BETA14,-Galactosyltransferase Mutant ARG228LYS in Complex with Alpha-Lactalbumin in the Presence of Udp-Galactose and Mn also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of BETA14,-Galactosyltransferase Mutant ARG228LYS in Complex with Alpha-Lactalbumin in the Presence of Udp-Galactose and Mn (pdb code 1yro). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of BETA14,-Galactosyltransferase Mutant ARG228LYS in Complex with Alpha-Lactalbumin in the Presence of Udp-Galactose and Mn, PDB code: 1yro:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1yro

Go back to Calcium Binding Sites List in 1yro
Calcium binding site 1 out of 2 in the Crystal Structure of BETA14,-Galactosyltransferase Mutant ARG228LYS in Complex with Alpha-Lactalbumin in the Presence of Udp-Galactose and Mn


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of BETA14,-Galactosyltransferase Mutant ARG228LYS in Complex with Alpha-Lactalbumin in the Presence of Udp-Galactose and Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca124

b:21.4
occ:1.00
O A:GLU84 2.2 20.2 1.0
O A:LYS79 2.3 20.7 1.0
OD1 A:ASP87 2.3 20.1 1.0
O A:HOH905 2.3 19.8 1.0
OD2 A:ASP88 2.4 18.6 1.0
OD1 A:ASP82 2.4 23.6 1.0
O A:HOH942 2.5 21.8 1.0
CG A:ASP82 3.3 24.5 1.0
CG A:ASP87 3.3 21.8 1.0
C A:GLU84 3.4 21.2 1.0
CG A:ASP88 3.5 21.5 1.0
OD2 A:ASP82 3.5 24.6 1.0
C A:LYS79 3.5 20.6 1.0
OD2 A:ASP87 3.6 21.1 1.0
OD1 A:ASP88 3.9 19.6 1.0
CA A:LEU80 4.2 19.9 1.0
CA A:GLU84 4.3 20.2 1.0
N A:GLU84 4.3 20.9 1.0
N A:LEU80 4.3 19.4 1.0
N A:LEU85 4.4 21.9 1.0
N A:ASP88 4.4 18.8 1.0
O A:HOH1351 4.4 34.4 1.0
O A:ASP82 4.4 25.3 1.0
CB A:GLU84 4.4 21.4 1.0
CA A:LEU85 4.5 22.3 1.0
N A:ASP82 4.5 25.0 1.0
CA A:LYS79 4.6 20.7 1.0
CB A:ASP82 4.6 22.9 1.0
C A:LEU80 4.7 21.1 1.0
C A:ASP82 4.7 26.4 1.0
CB A:ASP88 4.7 20.1 1.0
CB A:ASP87 4.7 19.2 1.0
CA A:ASP82 4.9 24.6 1.0
N A:ASP87 4.9 19.8 1.0
C A:LEU85 4.9 22.6 1.0
N A:LEU81 4.9 20.0 1.0
CB A:LYS79 4.9 22.9 1.0
O A:HOH1007 5.0 26.0 1.0
CD2 A:LEU80 5.0 22.3 1.0

Calcium binding site 2 out of 2 in 1yro

Go back to Calcium Binding Sites List in 1yro
Calcium binding site 2 out of 2 in the Crystal Structure of BETA14,-Galactosyltransferase Mutant ARG228LYS in Complex with Alpha-Lactalbumin in the Presence of Udp-Galactose and Mn


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of BETA14,-Galactosyltransferase Mutant ARG228LYS in Complex with Alpha-Lactalbumin in the Presence of Udp-Galactose and Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca124

b:26.1
occ:1.00
O C:GLU84 2.2 28.6 1.0
O C:LYS79 2.3 22.4 1.0
O C:HOH908 2.3 21.2 1.0
OD1 C:ASP87 2.3 26.0 1.0
OD2 C:ASP88 2.4 20.1 1.0
OD1 C:ASP82 2.4 30.7 1.0
O C:HOH933 2.5 30.0 1.0
CG C:ASP87 3.4 26.1 1.0
CG C:ASP82 3.4 29.9 1.0
C C:GLU84 3.4 29.2 1.0
C C:LYS79 3.5 22.9 1.0
CG C:ASP88 3.5 21.3 1.0
OD2 C:ASP87 3.7 25.7 1.0
OD2 C:ASP82 3.7 29.7 1.0
OD1 C:ASP88 4.0 21.1 1.0
O C:HOH1131 4.0 30.5 1.0
CA C:LEU80 4.1 20.8 1.0
CB C:GLU84 4.1 33.5 1.0
N C:LEU80 4.2 22.4 1.0
CA C:GLU84 4.2 30.6 1.0
N C:GLU84 4.3 29.5 1.0
O C:ASP82 4.4 29.9 1.0
N C:LEU85 4.4 27.9 1.0
N C:ASP88 4.4 21.2 1.0
CA C:LEU85 4.4 26.4 1.0
N C:ASP82 4.5 26.5 1.0
C C:LEU80 4.6 23.1 1.0
CA C:LYS79 4.6 24.1 1.0
C C:ASP82 4.7 30.7 1.0
CB C:ASP82 4.7 28.9 1.0
CB C:ASP87 4.8 25.2 1.0
CB C:ASP88 4.8 19.0 1.0
CD2 C:LEU80 4.8 16.8 1.0
N C:LEU81 4.9 21.0 1.0
N C:ASP87 4.9 23.7 1.0
CA C:ASP82 4.9 30.2 1.0
C C:LEU85 4.9 26.4 1.0
CB C:LYS79 4.9 24.4 1.0

Reference:

B.Ramakrishnan, E.Boeggeman, P.K.Qasba. Mutation of Arginine 228 to Lysine Enhances the Glucosyltransferase Activity of Bovine Beta-1,4-Galactosyltransferase I Biochemistry V. 44 3202 2005.
ISSN: ISSN 0006-2960
PubMed: 15736931
DOI: 10.1021/BI0479454
Page generated: Fri Jul 12 08:10:34 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy