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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: Sat Dec 12 03:29:07 2020

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