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Manganese 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:

Calcium (Ca) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese 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 Manganese atom.
In total 2 binding sites of Manganese 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 Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1yro

Go back to Manganese Binding Sites List in 1yro
Manganese 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 Manganese with other atoms in the Mn 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
B:Mn404

b:25.2
occ:1.00
O1A B:GDU403 2.0 23.8 1.0
OD2 B:ASP254 2.2 24.7 1.0
O2B B:GDU403 2.2 25.4 1.0
NE2 B:HIS347 2.2 28.6 1.0
O B:HOH909 2.2 20.1 1.0
SD B:MET344 2.8 27.6 1.0
CE1 B:HIS347 3.1 31.2 1.0
CG B:ASP254 3.2 25.3 1.0
CD2 B:HIS347 3.2 31.2 1.0
PA B:GDU403 3.3 25.7 1.0
OD1 B:ASP254 3.5 23.9 1.0
PB B:GDU403 3.5 27.9 1.0
O3A B:GDU403 3.6 27.9 1.0
CG B:MET344 3.7 27.1 1.0
O3D B:GDU403 3.9 23.0 1.0
O3B B:GDU403 4.0 29.3 1.0
CE B:MET344 4.0 27.8 1.0
O2A B:GDU403 4.0 29.5 1.0
O B:HOH964 4.1 29.0 1.0
ND1 B:HIS347 4.3 30.7 1.0
CG B:HIS347 4.3 31.3 1.0
O5D B:GDU403 4.4 27.8 1.0
NH2 B:ARG191 4.5 29.1 1.0
O1B B:GDU403 4.5 31.4 1.0
CB B:ASP254 4.5 25.6 1.0
OD2 B:ASP252 4.5 23.3 1.0
O B:HOH1217 4.6 34.8 1.0
NH1 B:ARG191 4.6 27.7 1.0
C5D B:GDU403 4.7 23.7 1.0
NZ B:LYS279 4.8 33.7 1.0
C3D B:GDU403 4.8 21.2 1.0

Manganese binding site 2 out of 2 in 1yro

Go back to Manganese Binding Sites List in 1yro
Manganese 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 Manganese with other atoms in the Mn 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
D:Mn529

b:21.7
occ:1.00
O2B D:GDU528 2.1 24.6 1.0
O1A D:GDU528 2.2 22.6 1.0
OD2 D:ASP254 2.2 20.4 1.0
NE2 D:HIS347 2.2 24.7 1.0
O D:HOH913 2.3 22.8 1.0
SD D:MET344 2.8 24.8 1.0
CG D:ASP254 3.2 20.9 1.0
CE1 D:HIS347 3.2 25.8 1.0
CD2 D:HIS347 3.2 24.1 1.0
PA D:GDU528 3.4 24.0 1.0
PB D:GDU528 3.4 24.5 1.0
OD1 D:ASP254 3.4 21.2 1.0
O3A D:GDU528 3.6 24.8 1.0
CE D:MET344 3.6 28.7 1.0
CG D:MET344 3.8 22.4 1.0
O D:HOH1050 3.8 35.5 1.0
O3B D:GDU528 3.9 28.6 1.0
O3D D:GDU528 3.9 20.2 1.0
O2A D:GDU528 4.1 27.2 1.0
ND1 D:HIS347 4.3 24.8 1.0
CG D:HIS347 4.4 26.8 1.0
NH2 D:ARG191 4.4 24.8 1.0
NH1 D:ARG191 4.5 21.2 1.0
O1B D:GDU528 4.5 30.2 1.0
CB D:ASP254 4.5 20.0 1.0
O5D D:GDU528 4.6 23.6 1.0
OD2 D:ASP252 4.7 20.4 1.0
C3D D:GDU528 4.7 20.4 1.0
C5D D:GDU528 4.8 21.9 1.0
CZ D:ARG191 4.9 24.0 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: Tue Dec 15 03:58:28 2020

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