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Manganese in PDB 1x7n: The Crystal Structure of Pyrococcus Furiosus Phosphoglucose Isomerase with Bound 5-Phospho-D-Arabinonate and Manganese

Enzymatic activity of The Crystal Structure of Pyrococcus Furiosus Phosphoglucose Isomerase with Bound 5-Phospho-D-Arabinonate and Manganese

All present enzymatic activity of The Crystal Structure of Pyrococcus Furiosus Phosphoglucose Isomerase with Bound 5-Phospho-D-Arabinonate and Manganese:
5.3.1.9;

Protein crystallography data

The structure of The Crystal Structure of Pyrococcus Furiosus Phosphoglucose Isomerase with Bound 5-Phospho-D-Arabinonate and Manganese, PDB code: 1x7n was solved by J.M.Berrisford, J.Akerboom, S.Brouns, S.E.Sedelnikova, A.P.Turnbull, J.Vander Oost, L.Salmon, R.Hardre, I.A.Murray, G.M.Blackburn, D.W.Rice, P.J.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.39 / 1.89
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 84.674, 42.382, 57.255, 90.00, 120.57, 90.00
R / Rfree (%) 14.1 / 21.2

Manganese Binding Sites:

The binding sites of Manganese atom in the The Crystal Structure of Pyrococcus Furiosus Phosphoglucose Isomerase with Bound 5-Phospho-D-Arabinonate and Manganese (pdb code 1x7n). 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 The Crystal Structure of Pyrococcus Furiosus Phosphoglucose Isomerase with Bound 5-Phospho-D-Arabinonate and Manganese, PDB code: 1x7n:

Manganese binding site 1 out of 1 in 1x7n

Go back to Manganese Binding Sites List in 1x7n
Manganese binding site 1 out of 1 in the The Crystal Structure of Pyrococcus Furiosus Phosphoglucose Isomerase with Bound 5-Phospho-D-Arabinonate and Manganese


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Crystal Structure of Pyrococcus Furiosus Phosphoglucose Isomerase with Bound 5-Phospho-D-Arabinonate and Manganese within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn400

b:36.2
occ:1.00
 O A:HOH407 2.3 24.9 1.0
OE1 A:GLU97 2.3 23.8 1.0
NE2 A:HIS136 2.3 26.7 1.0
NE2 A:HIS88 2.4 22.4 1.0
O1 A:PA5301 2.4 19.8 1.0
NE2 A:HIS90 2.7 23.9 1.0
CE1 A:HIS136 3.1 39.4 1.0
CE1 A:HIS88 3.2 31.0 1.0
CD A:GLU97 3.3 19.4 1.0
C1 A:PA5301 3.3 26.2 1.0
CD2 A:HIS90 3.4 26.6 1.0
CD2 A:HIS136 3.5 27.3 1.0
CD2 A:HIS88 3.5 26.7 1.0
O1A A:PA5301 3.5 24.7 1.0
CE1 A:HIS90 3.7 25.6 1.0
OE2 A:GLU97 3.7 35.1 1.0
ND1 A:HIS136 4.3 31.1 1.0
ND1 A:HIS88 4.3 28.6 1.0
O A:HOH566 4.4 26.5 1.0
O A:HOH404 4.5 36.4 1.0
CG A:HIS136 4.5 25.0 1.0
CG A:HIS88 4.5 23.4 1.0
CG A:HIS90 4.6 28.5 1.0
CG A:GLU97 4.6 30.8 1.0
ND1 A:HIS90 4.7 30.1 1.0
OH A:TYR99 4.7 30.4 1.0
C2 A:PA5301 4.7 17.4 1.0
CB A:GLU97 4.9 23.1 1.0
CD2 A:HIS158 4.9 33.5 1.0
NE2 A:HIS158 4.9 30.4 1.0
O3 A:PA5301 5.0 26.7 1.0

Reference:

J.M.Berrisford, J.Akerboom, S.Brouns, S.E.Sedelnikova, A.P.Turnbull, J.Van Der Oost, L.Salmon, R.Hardre, I.A.Murray, G.M.Blackburn, D.W.Rice, P.J.Baker. The Structures of Inhibitor Complexes of Pyrococcus Furiosus Phosphoglucose Isomerase Provide Insights Into Substrate Binding and Catalysis. J.Mol.Biol. V. 343 649 2004.
ISSN: ISSN 0022-2836
PubMed: 15465052
DOI: 10.1016/J.JMB.2004.08.061
Page generated: Sat Oct 5 12:59:56 2024

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