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Manganese in PDB 1nvk: T4 Phage Bgt in Complex with Udp and A MN2+ Ion at 1.8 A Resolution

Enzymatic activity of T4 Phage Bgt in Complex with Udp and A MN2+ Ion at 1.8 A Resolution

All present enzymatic activity of T4 Phage Bgt in Complex with Udp and A MN2+ Ion at 1.8 A Resolution:
2.4.1.27;

Protein crystallography data

The structure of T4 Phage Bgt in Complex with Udp and A MN2+ Ion at 1.8 A Resolution, PDB code: 1nvk was solved by L.Lariviere, J.Kurzeck, V.Gueguen-Chaignon, W.Rueger, S.Morera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.808, 71.400, 62.000, 90.00, 91.65, 90.00
R / Rfree (%) 17.4 / 21

Manganese Binding Sites:

The binding sites of Manganese atom in the T4 Phage Bgt in Complex with Udp and A MN2+ Ion at 1.8 A Resolution (pdb code 1nvk). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the T4 Phage Bgt in Complex with Udp and A MN2+ Ion at 1.8 A Resolution, PDB code: 1nvk:

Manganese binding site 1 out of 1 in 1nvk

Go back to Manganese Binding Sites List in 1nvk
Manganese binding site 1 out of 1 in the T4 Phage Bgt in Complex with Udp and A MN2+ Ion at 1.8 A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of T4 Phage Bgt in Complex with Udp and A MN2+ Ion at 1.8 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn701

b:21.6
occ:1.00
O A:HOH964 2.2 14.8 1.0
O A:HOH1106 2.2 20.3 1.0
O A:HOH1118 2.3 17.9 1.0
O1B A:UDP700 2.3 9.7 1.0
O A:HOH717 2.3 9.8 1.0
O A:HOH1119 2.4 15.6 1.0
PB A:UDP700 3.5 9.8 1.0
O2B A:UDP700 3.6 9.5 1.0
O A:HOH1116 3.6 36.3 1.0
OE1 A:GLU163 4.0 12.7 1.0
O A:HOH772 4.0 14.2 1.0
O2A A:UDP700 4.1 9.2 1.0
O A:THR99 4.3 10.6 1.0
OE2 A:GLU163 4.3 13.1 1.0
O5' A:UDP700 4.3 11.0 1.0
O3A A:UDP700 4.4 8.6 1.0
O A:HOH912 4.5 25.1 1.0
CD A:GLU163 4.6 14.1 1.0
PA A:UDP700 4.6 10.1 1.0
O3B A:UDP700 4.6 10.7 1.0
OD1 A:ASP100 4.6 11.9 1.0
O A:HOH965 4.7 24.2 1.0
OH A:TYR261 4.8 12.3 1.0
NH1 A:ARG191 4.9 11.7 1.0
CB A:ASP100 4.9 9.4 1.0
CG A:ASP100 5.0 11.1 1.0
C5' A:UDP700 5.0 10.8 1.0

Reference:

L.Lariviere, V.Gueguen-Chaignon, S.Morera. Crystal Structures of the T4 Phage Beta-Glucosyltransferase and the D100A Mutant in Complex with Udp-Glucose: Glucose Binding and Identification of the Catalytic Base For A Direct Displacement Mechanism J.Mol.Biol. V. 330 1077 2003.
ISSN: ISSN 0022-2836
PubMed: 12860129
DOI: 10.1016/S0022-2836(03)00635-1
Page generated: Sat Oct 5 11:53:11 2024

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