Calcium in PDB 1o23: Crystal Structure of Lactose Synthase in the Presence of Udp-Glucose

All present enzymatic activity of Crystal Structure of Lactose Synthase in the Presence of Udp-Glucose:
2.4.1.90;

The structure of Crystal Structure of Lactose Synthase in the Presence of Udp-Glucose, PDB code: 1o23 was solved by B.Ramakrishnan, P.S.Shah, P.K.Qasba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 2.32
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	55.545, 99.379, 102.568, 90.00, 104.09, 90.00
R / Rfree (%)	20.1 / 26.5

The structure of Crystal Structure of Lactose Synthase in the Presence of Udp-Glucose also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Calcium atom in the Crystal Structure of Lactose Synthase in the Presence of Udp-Glucose (pdb code 1o23). 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 Lactose Synthase in the Presence of Udp-Glucose, PDB code: 1o23:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Lactose Synthase in the Presence of Udp-Glucose


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 Lactose Synthase in the Presence of Udp-Glucose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca805 b:42.6 occ:1.00 O A:GLU84 2.1 43.9 1.0 OD1 A:ASP87 2.3 41.0 1.0 O A:LYS79 2.3 41.7 1.0 OD2 A:ASP88 2.4 42.0 1.0 O A:HOH903 2.6 30.9 1.0 O A:HOH912 2.6 41.4 1.0 OD1 A:ASP82 2.8 53.3 1.0 CG A:ASP87 3.2 41.9 1.0 C A:GLU84 3.3 45.1 1.0 OD2 A:ASP87 3.4 40.0 1.0 CG A:ASP82 3.5 51.8 1.0 C A:LYS79 3.5 44.6 1.0 CG A:ASP88 3.6 36.7 1.0 OD2 A:ASP82 3.6 54.7 1.0 OD1 A:ASP88 4.0 39.0 1.0 CA A:LEU80 4.1 45.5 1.0 CA A:GLU84 4.2 45.5 1.0 N A:GLU84 4.2 44.4 1.0 N A:LEU80 4.3 43.6 1.0 N A:LEU85 4.3 45.5 1.0 CB A:GLU84 4.4 46.6 1.0 N A:ASP88 4.4 37.8 1.0 CA A:LEU85 4.5 46.5 1.0 C A:LEU80 4.6 47.0 1.0 CB A:ASP87 4.6 39.9 1.0 CA A:LYS79 4.7 45.8 1.0 N A:ASP82 4.7 45.8 1.0 N A:ASP87 4.8 40.1 1.0 CB A:ASP88 4.8 36.9 1.0 CB A:ASP82 4.8 48.1 1.0 C A:LEU85 4.8 46.1 1.0 O A:ASP82 4.9 45.9 1.0 C A:ASP82 4.9 45.8 1.0 CD2 A:LEU80 4.9 37.6 1.0 CB A:LYS79 4.9 49.0 1.0 N A:LEU81 5.0 46.0 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Lactose Synthase in the Presence of Udp-Glucose


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 Lactose Synthase in the Presence of Udp-Glucose within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca806 b:36.6 occ:1.00 O C:HOH911 2.2 35.7 1.0 O C:LYS481 2.3 35.9 1.0 O C:GLU486 2.3 41.7 1.0 OD1 C:ASP489 2.3 36.1 1.0 OD2 C:ASP490 2.4 32.5 1.0 O C:HOH944 2.4 38.4 1.0 OD1 C:ASP484 2.5 36.6 1.0 CG C:ASP484 3.3 36.5 1.0 CG C:ASP489 3.3 37.2 1.0 C C:GLU486 3.4 41.8 1.0 OD2 C:ASP484 3.5 36.1 1.0 C C:LYS481 3.5 35.0 1.0 OD2 C:ASP489 3.5 37.6 1.0 CG C:ASP490 3.6 33.3 1.0 OD1 C:ASP490 4.1 33.4 1.0 CA C:LEU482 4.2 33.0 1.0 O C:ASP484 4.3 37.2 1.0 N C:LEU482 4.3 34.3 1.0 N C:LEU487 4.3 42.3 1.0 CA C:GLU486 4.3 41.1 1.0 N C:GLU486 4.4 39.7 1.0 N C:ASP490 4.4 32.6 1.0 CA C:LEU487 4.4 42.4 1.0 CA C:LYS481 4.5 33.9 1.0 CB C:GLU486 4.5 41.7 1.0 N C:ASP484 4.6 35.2 1.0 CB C:ASP484 4.6 34.8 1.0 C C:ASP484 4.7 36.3 1.0 CB C:ASP489 4.7 36.2 1.0 C C:LEU482 4.8 32.9 1.0 CB C:ASP490 4.8 33.1 1.0 N C:ASP489 4.8 41.1 1.0 CD1 C:LEU487 4.8 41.3 1.0 CB C:LYS481 4.9 35.6 1.0 CD2 C:LEU482 4.9 29.4 1.0 C C:LEU487 4.9 44.4 1.0 CA C:ASP484 4.9 35.1 1.0 O C:HOH1108 4.9 42.5 1.0 N C:LEU483 4.9 32.6 1.0

B.Ramakrishnan, P.S.Shah, P.K.Qasba. Alpha-Lactalbumin (La) Stimulates Milk Beta-1,4-Galactosyltransferase I (Beta 4GAL-T1) to Transfer Glucose From Udp-Glucose to N-Acetylglucosamine. Crystal Structure of Beta 4GAL-T1 X La Complex with Udp-Glc. J.Biol.Chem. V. 276 37665 2001.
ISSN: ISSN 0021-9258
PubMed: 11485999
DOI: 10.1074/JBC.M102458200