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Manganese in PDB 3pe7: Oligogalacturonate Lyase in Complex with Manganese

Protein crystallography data

The structure of Oligogalacturonate Lyase in Complex with Manganese, PDB code: 3pe7 was solved by D.W.Abbott, H.J.Gilbert, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.650, 75.510, 78.510, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.7

Other elements in 3pe7:

The structure of Oligogalacturonate Lyase in Complex with Manganese also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Oligogalacturonate Lyase in Complex with Manganese (pdb code 3pe7). 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 Oligogalacturonate Lyase in Complex with Manganese, PDB code: 3pe7:

Manganese binding site 1 out of 1 in 3pe7

Go back to Manganese Binding Sites List in 3pe7
Manganese binding site 1 out of 1 in the Oligogalacturonate Lyase in 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 Oligogalacturonate Lyase in Complex with Manganese within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn389

b:7.5
occ:1.00
OXT A:ACT392 2.1 18.1 1.0
NE2 A:HIS355 2.1 7.9 1.0
OE1 A:GLN350 2.1 9.8 1.0
NE2 A:HIS287 2.1 10.0 1.0
ND1 A:HIS353 2.1 9.3 1.0
O A:ACT392 2.2 18.3 1.0
C A:ACT392 2.5 19.5 1.0
CE1 A:HIS287 3.0 9.2 1.0
CE1 A:HIS353 3.0 9.0 1.0
CE1 A:HIS355 3.1 9.4 1.0
CD2 A:HIS355 3.1 8.4 1.0
CD2 A:HIS287 3.2 8.4 1.0
CD A:GLN350 3.2 11.2 1.0
CG A:HIS353 3.2 8.2 1.0
NE2 A:GLN350 3.6 11.8 1.0
CB A:HIS353 3.6 7.9 1.0
CH3 A:ACT392 4.0 20.5 1.0
ND1 A:HIS287 4.1 9.0 1.0
NE2 A:HIS353 4.2 10.2 1.0
ND1 A:HIS355 4.2 8.2 1.0
CG A:HIS287 4.2 8.3 1.0
CG A:HIS355 4.2 7.5 1.0
O A:HOH849 4.3 37.3 1.0
CD2 A:HIS353 4.3 8.1 1.0
O A:HOH426 4.4 35.6 1.0
CG A:GLN350 4.5 11.1 1.0
CB A:GLN350 4.9 10.2 1.0

Reference:

D.W.Abbott, H.J.Gilbert, A.B.Boraston. The Active Site of Oligogalacturonate Lyase Provides Unique Insights Into Cytoplasmic Oligogalacturonate Beta-Elimination. J.Biol.Chem. V. 285 39029 2010.
ISSN: ISSN 0021-9258
PubMed: 20851883
DOI: 10.1074/JBC.M110.153981
Page generated: Tue Dec 15 04:13:48 2020

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