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Manganese in PDB 2fya: Crystal Structure of the Catalytic Domain of the Human BETA1, 4-Galactosyltransferase Mutant M339H Complex with Manganese

Enzymatic activity of Crystal Structure of the Catalytic Domain of the Human BETA1, 4-Galactosyltransferase Mutant M339H Complex with Manganese

All present enzymatic activity of Crystal Structure of the Catalytic Domain of the Human BETA1, 4-Galactosyltransferase Mutant M339H Complex with Manganese:
2.4.1.90;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of the Human BETA1, 4-Galactosyltransferase Mutant M339H Complex with Manganese, PDB code: 2fya was solved by B.Ramakrishnan, V.Ramasamy, P.K.Qasba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.93 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 70.480, 137.490, 66.110, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 22.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Catalytic Domain of the Human BETA1, 4-Galactosyltransferase Mutant M339H Complex with Manganese (pdb code 2fya). 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 the Catalytic Domain of the Human BETA1, 4-Galactosyltransferase Mutant M339H Complex with Manganese, PDB code: 2fya:

Manganese binding site 1 out of 1 in 2fya

Go back to Manganese Binding Sites List in 2fya
Manganese binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of the Human BETA1, 4-Galactosyltransferase Mutant M339H Complex with Manganese


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 the Catalytic Domain of the Human BETA1, 4-Galactosyltransferase Mutant M339H Complex with Manganese within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn403

b:35.8
occ:1.00
 O A:HOH577 2.0 33.1 1.0
NE2 A:HIS340 2.2 25.5 1.0
O A:HOH699 2.2 25.8 1.0
OD2 A:ASP250 2.3 21.3 1.0
O A:HOH719 2.4 25.6 1.0
O A:HOH722 2.4 46.9 1.0
CE1 A:HIS340 3.1 24.0 1.0
CG A:ASP250 3.2 22.9 1.0
CD2 A:HIS340 3.3 23.4 1.0
O A:HOH823 3.8 51.5 1.0
OD1 A:ASP250 3.9 25.4 1.0
O A:HOH723 4.1 25.7 1.0
O A:ILE341 4.1 28.9 1.0
O A:HOH615 4.1 30.9 1.0
CB A:ASP250 4.2 21.0 1.0
ND1 A:HIS340 4.3 25.4 1.0
O A:HOH712 4.3 35.1 1.0
CG A:HIS340 4.4 24.7 1.0
O A:HOH817 4.5 60.4 1.0
NZ A:LYS275 4.7 39.4 1.0
NH1 A:ARG187 4.7 38.5 1.0
O A:HOH851 4.9 61.6 1.0
O A:HOH839 4.9 60.1 1.0

Reference:

B.Ramakrishnan, V.Ramasamy, P.K.Qasba. Structural Snapshots of Beta-1,4-Galactosyltransferase-I Along the Kinetic Pathway. J.Mol.Biol. V. 357 1619 2006.
ISSN: ISSN 0022-2836
PubMed: 16497331
DOI: 10.1016/J.JMB.2006.01.088
Page generated: Sat Oct 5 14:08:13 2024

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