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Manganese in PDB 1oqm: A 1:1 Complex Between Alpha-Lactalbumin and BETA1,4- Galactosyltransferase in the Presence of Udp-N-Acetyl- Galactosamine

Enzymatic activity of A 1:1 Complex Between Alpha-Lactalbumin and BETA1,4- Galactosyltransferase in the Presence of Udp-N-Acetyl- Galactosamine

All present enzymatic activity of A 1:1 Complex Between Alpha-Lactalbumin and BETA1,4- Galactosyltransferase in the Presence of Udp-N-Acetyl- Galactosamine:
2.4.1.38;

Protein crystallography data

The structure of A 1:1 Complex Between Alpha-Lactalbumin and BETA1,4- Galactosyltransferase in the Presence of Udp-N-Acetyl- Galactosamine, PDB code: 1oqm was solved by B.Ramakrishnan, P.K.Qasba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.56 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 57.471, 95.677, 100.581, 90.00, 101.40, 90.00
R / Rfree (%) 19.4 / 24.4

Other elements in 1oqm:

The structure of A 1:1 Complex Between Alpha-Lactalbumin and BETA1,4- Galactosyltransferase in the Presence of Udp-N-Acetyl- Galactosamine also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the A 1:1 Complex Between Alpha-Lactalbumin and BETA1,4- Galactosyltransferase in the Presence of Udp-N-Acetyl- Galactosamine (pdb code 1oqm). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the A 1:1 Complex Between Alpha-Lactalbumin and BETA1,4- Galactosyltransferase in the Presence of Udp-N-Acetyl- Galactosamine, PDB code: 1oqm:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1oqm

Go back to Manganese Binding Sites List in 1oqm
Manganese binding site 1 out of 2 in the A 1:1 Complex Between Alpha-Lactalbumin and BETA1,4- Galactosyltransferase in the Presence of Udp-N-Acetyl- Galactosamine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of A 1:1 Complex Between Alpha-Lactalbumin and BETA1,4- Galactosyltransferase in the Presence of Udp-N-Acetyl- Galactosamine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn403

b:31.2
occ:1.00
 O1A B:UD2404 2.2 30.3 1.0
OD2 B:ASP254 2.2 30.4 1.0
O2B B:UD2404 2.3 25.6 1.0
NE2 B:HIS347 2.4 47.4 1.0
O B:HOH989 2.5 27.9 1.0
SD B:MET344 2.9 34.3 1.0
CG B:ASP254 3.1 29.4 1.0
CE1 B:HIS347 3.2 47.6 1.0
CD2 B:HIS347 3.4 46.1 1.0
OD1 B:ASP254 3.4 29.1 1.0
PA B:UD2404 3.4 31.2 1.0
PB B:UD2404 3.5 30.5 1.0
O3A B:UD2404 3.8 30.8 1.0
O3B B:UD2404 3.8 23.8 1.0
CE B:MET344 3.9 33.1 1.0
CG B:MET344 3.9 31.1 1.0
O1' B:UD2404 4.0 29.4 1.0
O2A B:UD2404 4.2 34.0 1.0
ND1 B:HIS347 4.4 46.3 1.0
CG B:HIS347 4.5 46.3 1.0
CB B:ASP254 4.5 30.6 1.0
O5B B:UD2404 4.5 33.8 1.0
C3B B:UD2404 4.6 28.3 1.0
C5B B:UD2404 4.7 30.8 1.0
OD2 B:ASP252 4.7 27.2 1.0
O1B B:UD2404 4.7 30.1 1.0
NH2 B:ARG191 4.8 42.5 1.0
NH1 B:ARG191 4.8 40.6 1.0
C8' B:UD2404 5.0 41.8 1.0

Manganese binding site 2 out of 2 in 1oqm

Go back to Manganese Binding Sites List in 1oqm
Manganese binding site 2 out of 2 in the A 1:1 Complex Between Alpha-Lactalbumin and BETA1,4- Galactosyltransferase in the Presence of Udp-N-Acetyl- Galactosamine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of A 1:1 Complex Between Alpha-Lactalbumin and BETA1,4- Galactosyltransferase in the Presence of Udp-N-Acetyl- Galactosamine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn403

b:29.2
occ:1.00
 O D:HOH927 2.1 26.6 1.0
O1A D:UD2528 2.1 29.0 1.0
O2B D:UD2528 2.2 23.9 1.0
NE2 D:HIS347 2.3 29.9 1.0
OD2 D:ASP254 2.3 23.5 1.0
SD D:MET344 2.9 27.6 1.0
CE1 D:HIS347 3.2 29.7 1.0
CG D:ASP254 3.2 23.8 1.0
PA D:UD2528 3.3 27.7 1.0
CD2 D:HIS347 3.3 28.2 1.0
OD1 D:ASP254 3.4 24.8 1.0
PB D:UD2528 3.4 25.7 1.0
CE D:MET344 3.5 24.9 1.0
O3A D:UD2528 3.7 26.4 1.0
CG D:MET344 3.8 26.5 1.0
O D:HOH945 3.8 30.6 1.0
O1' D:UD2528 3.9 25.2 1.0
O3B D:UD2528 3.9 26.6 1.0
O2A D:UD2528 4.1 30.1 1.0
ND1 D:HIS347 4.3 31.0 1.0
CG D:HIS347 4.4 30.9 1.0
O D:HOH1079 4.5 47.3 1.0
O5B D:UD2528 4.5 26.2 1.0
NH1 D:ARG191 4.5 34.9 1.0
NH2 D:ARG191 4.5 36.0 1.0
OD2 D:ASP252 4.6 28.5 1.0
CB D:ASP254 4.6 25.3 1.0
C3B D:UD2528 4.7 23.5 1.0
O1B D:UD2528 4.7 29.3 1.0
C5B D:UD2528 4.7 25.5 1.0

Reference:

B.Ramakrishnan, P.K.Qasba. Structure-Based Design of Beta 1,4-Galactosyltransferase I (Beta 4GAL-T1) with Equally Efficient N-Acetylgalactosaminyltransferase Activity: Point Mutation Broadens Beta 4GAL-T1 Donor Specificity. J.Biol.Chem. V. 277 20833 2002.
ISSN: ISSN 0021-9258
PubMed: 11916963
DOI: 10.1074/JBC.M111183200
Page generated: Sat Oct 5 12:01:04 2024

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