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Manganese in PDB 4lw6: Crystal Structure of Catalytic Domain of Drosophila BETA1, 4GALACTOSYLTRANSFERASE 7 Complex with Xylobiose

Enzymatic activity of Crystal Structure of Catalytic Domain of Drosophila BETA1, 4GALACTOSYLTRANSFERASE 7 Complex with Xylobiose

All present enzymatic activity of Crystal Structure of Catalytic Domain of Drosophila BETA1, 4GALACTOSYLTRANSFERASE 7 Complex with Xylobiose:
2.4.1.133;

Protein crystallography data

The structure of Crystal Structure of Catalytic Domain of Drosophila BETA1, 4GALACTOSYLTRANSFERASE 7 Complex with Xylobiose, PDB code: 4lw6 was solved by P.K.Qasba, B.Ramakrishnan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.00 / 2.40
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 81.943, 81.943, 133.053, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 21.5

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Catalytic Domain of Drosophila BETA1, 4GALACTOSYLTRANSFERASE 7 Complex with Xylobiose (pdb code 4lw6). 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 Crystal Structure of Catalytic Domain of Drosophila BETA1, 4GALACTOSYLTRANSFERASE 7 Complex with Xylobiose, PDB code: 4lw6:

Manganese binding site 1 out of 1 in 4lw6

Go back to Manganese Binding Sites List in 4lw6
Manganese binding site 1 out of 1 in the Crystal Structure of Catalytic Domain of Drosophila BETA1, 4GALACTOSYLTRANSFERASE 7 Complex with Xylobiose


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 Catalytic Domain of Drosophila BETA1, 4GALACTOSYLTRANSFERASE 7 Complex with Xylobiose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:44.0
occ:1.00
O1B A:UDP402 2.1 45.2 1.0
O1A A:UDP402 2.2 47.2 1.0
OD2 A:ASP147 2.2 44.5 1.0
O A:HOH568 2.3 48.7 1.0
ND1 A:HIS243 2.3 49.2 1.0
NE2 A:HIS241 2.4 42.9 1.0
CG A:ASP147 3.1 45.6 1.0
CE1 A:HIS243 3.2 41.8 1.0
OD1 A:ASP147 3.2 41.3 1.0
PB A:UDP402 3.3 45.5 1.0
CE1 A:HIS241 3.3 45.5 1.0
CG A:HIS243 3.3 48.6 1.0
CD2 A:HIS241 3.4 43.7 1.0
PA A:UDP402 3.4 49.4 1.0
O3A A:UDP402 3.6 57.1 1.0
CB A:HIS243 3.7 47.1 1.0
O3' A:UDP402 3.9 42.9 1.0
O3B A:UDP402 4.0 51.2 1.0
NH2 A:ARG250 4.0 42.4 1.0
O2A A:UDP402 4.2 47.7 1.0
O A:HOH596 4.3 51.1 1.0
NE2 A:HIS243 4.3 46.7 1.0
O2B A:UDP402 4.4 42.6 1.0
CD2 A:HIS243 4.4 43.6 1.0
ND1 A:HIS241 4.4 50.5 1.0
CB A:ASP147 4.5 43.2 1.0
CG A:HIS241 4.5 49.8 1.0
O5' A:UDP402 4.6 50.7 1.0
C3' A:UDP402 4.7 46.0 1.0
C5' A:UDP402 4.9 42.4 1.0
OD2 A:ASP145 5.0 49.4 1.0
CZ A:ARG250 5.0 50.2 1.0

Reference:

Y.Tsutsui, B.Ramakrishnan, P.K.Qasba. Crystal Structures of Beta-1,4-Galactosyltransferase 7 Enzyme Reveal Conformational Changes and Substrate Binding. J.Biol.Chem. V. 288 31963 2013.
ISSN: ISSN 0021-9258
PubMed: 24052259
DOI: 10.1074/JBC.M113.509984
Page generated: Sat Oct 5 20:17:19 2024

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