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Magnesium in PDB 2bif: 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase H256A Mutant with F6P in Phosphatase Active Site

Enzymatic activity of 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase H256A Mutant with F6P in Phosphatase Active Site

All present enzymatic activity of 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase H256A Mutant with F6P in Phosphatase Active Site:
2.7.1.105; 3.1.3.46;

Protein crystallography data

The structure of 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase H256A Mutant with F6P in Phosphatase Active Site, PDB code: 2bif was solved by M.H.Yuen, C.A.Hasemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.40
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 61.740, 73.510, 76.700, 116.90, 99.31, 105.20
R / Rfree (%) 20 / 24.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase H256A Mutant with F6P in Phosphatase Active Site (pdb code 2bif). 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 H256A Mutant with F6P in Phosphatase Active Site, PDB code: 2bif:

Magnesium binding site 1 out of 1 in 2bif

Go back to Magnesium Binding Sites List in 2bif
Magnesium binding site 1 out of 1 in the 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase H256A Mutant with F6P in Phosphatase Active Site


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 H256A Mutant with F6P in Phosphatase Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:39.4
occ:1.00
 O1B A:ANP500 2.3 20.0 1.0
OG1 A:THR52 2.3 18.2 1.0
O1G A:ANP500 2.5 26.7 1.0
OD1 A:ASP128 2.7 15.8 1.0
OD2 A:ASP128 3.2 17.0 1.0
CG A:ASP128 3.3 15.6 1.0
PG A:ANP500 3.4 25.0 0.3
PB A:ANP500 3.5 24.6 1.0
O2G A:ANP500 3.6 23.3 0.3
O A:HOH957 3.7 52.4 1.0
CB A:THR52 3.7 17.7 1.0
N A:THR52 3.7 21.5 1.0
CE A:LYS51 3.8 9.3 1.0
CB A:LYS51 3.9 12.1 1.0
N3B A:ANP500 3.9 25.8 1.0
CA A:THR52 4.1 23.8 1.0
O2B A:ANP500 4.1 19.6 1.0
NZ A:LYS51 4.1 18.4 1.0
ND2 A:ASN73 4.2 34.8 1.0
C A:LYS51 4.4 17.8 1.0
CA A:LYS51 4.6 18.2 1.0
CG2 A:THR52 4.7 20.8 1.0
CB A:ASP128 4.7 13.9 1.0
O3G A:ANP500 4.8 24.5 0.3
CD A:LYS51 4.8 12.2 1.0
O3A A:ANP500 4.8 29.1 1.0
CG A:LYS51 4.9 12.9 1.0
O A:ASP128 4.9 20.3 1.0
C A:ASP128 4.9 18.0 1.0

Reference:

M.H.Yuen, H.Mizuguchi, Y.H.Lee, P.F.Cook, K.Uyeda, C.A.Hasemann. Crystal Structure of the H256A Mutant of Rat Testis Fructose-6-Phosphate,2-Kinase/Fructose-2,6- Bisphosphatase. Fructose 6-Phosphate in the Active Site Leads to Mechanisms For Both Mutant and Wild Type Bisphosphatase Activities. J.Biol.Chem. V. 274 2176 1999.
ISSN: ISSN 0021-9258
PubMed: 9890980
DOI: 10.1074/JBC.274.4.2176
Page generated: Tue Aug 13 21:54:16 2024

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