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Magnesium in PDB 1bif: 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase Bifunctional Enzyme Complexed with Atp-G-S and Phosphate

Enzymatic activity of 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase Bifunctional Enzyme Complexed with Atp-G-S and Phosphate

All present enzymatic activity of 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase Bifunctional Enzyme Complexed with Atp-G-S and Phosphate:
2.7.1.105; 3.1.3.46;

Protein crystallography data

The structure of 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase Bifunctional Enzyme Complexed with Atp-G-S and Phosphate, PDB code: 1bif was solved by C.A.Hasemann, J.Deisenhofer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.00
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 83.000, 83.000, 130.600, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 25

Magnesium Binding Sites:

The binding sites of Magnesium atom in the 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase Bifunctional Enzyme Complexed with Atp-G-S and Phosphate (pdb code 1bif). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase Bifunctional Enzyme Complexed with Atp-G-S and Phosphate, PDB code: 1bif:

Magnesium binding site 1 out of 1 in 1bif

Go back to Magnesium Binding Sites List in 1bif
Magnesium binding site 1 out of 1 in the 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase Bifunctional Enzyme Complexed with Atp-G-S and Phosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase Bifunctional Enzyme Complexed with Atp-G-S and Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:38.1
occ:1.00
 O2G A:AGS500 2.3 33.5 0.4
OD1 A:ASP128 2.7 23.9 1.0
OG1 A:THR52 2.9 25.4 1.0
O1B A:AGS500 2.9 19.9 1.0
PG A:AGS500 3.4 33.8 0.4
CG A:ASP128 3.4 17.0 1.0
OD2 A:ASP128 3.5 23.1 1.0
S1G A:AGS500 3.6 30.7 0.4
CE A:LYS51 3.7 24.5 1.0
CB A:LYS51 3.9 17.9 1.0
PB A:AGS500 4.0 25.9 1.0
N A:THR52 4.0 19.1 1.0
O A:HOH908 4.1 29.8 1.0
O3B A:AGS500 4.1 27.3 1.0
NZ A:LYS51 4.2 23.8 1.0
CB A:THR52 4.2 22.4 1.0
O A:HOH907 4.3 53.5 1.0
ND2 A:ASN73 4.4 39.9 1.0
CA A:THR52 4.5 21.9 1.0
O2B A:AGS500 4.5 22.3 1.0
O A:ASP128 4.6 22.5 1.0
C A:ASP128 4.6 20.2 1.0
N A:ALA129 4.6 22.4 1.0
O3G A:AGS500 4.7 33.6 0.4
C A:LYS51 4.7 18.3 1.0
CD A:LYS51 4.7 19.9 1.0
CB A:ASP128 4.8 19.4 1.0
CA A:ALA129 4.8 21.9 1.0
CA A:LYS51 4.9 18.1 1.0
CG A:LYS51 4.9 18.8 1.0
C A:ALA129 4.9 21.1 1.0
O A:HOH914 4.9 48.1 1.0

Reference:

C.A.Hasemann, E.S.Istvan, K.Uyeda, J.Deisenhofer. The Crystal Structure of the Bifunctional Enzyme 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase Reveals Distinct Domain Homologies. Structure V. 4 1017 1996.
ISSN: ISSN 0969-2126
PubMed: 8805587
DOI: 10.1016/S0969-2126(96)00109-8
Page generated: Tue Aug 13 02:13:24 2024

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