Atomistry » Manganese » PDB 1o9i-1pj3 » 1oqm
Atomistry »
  Manganese »
    PDB 1o9i-1pj3 »
      1oqm »

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: Tue Dec 15 03:54:01 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy