Manganese in PDB 1fsa: The T-State Structure of Lys 42 to Ala Mutant of the Pig Kidney Fructose 1,6-Bisphosphatase Expressed in E. Coli

All present enzymatic activity of The T-State Structure of Lys 42 to Ala Mutant of the Pig Kidney Fructose 1,6-Bisphosphatase Expressed in E. Coli:
3.1.3.11;

The structure of The T-State Structure of Lys 42 to Ala Mutant of the Pig Kidney Fructose 1,6-Bisphosphatase Expressed in E. Coli, PDB code: 1fsa was solved by G.Lu, B.Stec, E.Giroux, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.30
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	61.050, 166.720, 79.980, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 23.2

The binding sites of Manganese atom in the The T-State Structure of Lys 42 to Ala Mutant of the Pig Kidney Fructose 1,6-Bisphosphatase Expressed in E. Coli (pdb code 1fsa). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the The T-State Structure of Lys 42 to Ala Mutant of the Pig Kidney Fructose 1,6-Bisphosphatase Expressed in E. Coli, PDB code: 1fsa:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the The T-State Structure of Lys 42 to Ala Mutant of the Pig Kidney Fructose 1,6-Bisphosphatase Expressed in E. Coli


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The T-State Structure of Lys 42 to Ala Mutant of the Pig Kidney Fructose 1,6-Bisphosphatase Expressed in E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn339 b:50.3 occ:1.00 O1 A:F6P338 1.9 58.0 1.0 OE2 A:GLU280 2.1 16.0 1.0 OD2 A:ASP118 2.1 18.8 1.0 OD2 A:ASP121 2.2 38.9 1.0 O A:HOH342 2.2 16.4 1.0 OE1 A:GLU97 3.1 30.8 1.0 CD A:GLU280 3.1 18.7 1.0 CG A:ASP121 3.2 37.1 1.0 CG A:ASP118 3.2 16.6 1.0 C1 A:F6P338 3.5 42.1 1.0 OD1 A:ASP118 3.7 12.8 1.0 CB A:ASP121 3.8 32.2 1.0 CG A:GLU280 3.8 8.7 1.0 NH2 A:ARG276 3.8 29.6 1.0 CA A:ASP121 4.0 27.1 1.0 OE1 A:GLU280 4.0 20.3 1.0 OD1 A:ASP121 4.1 35.9 1.0 CD A:GLU97 4.2 31.0 1.0 O A:HOH341 4.2 25.7 1.0 O2 A:F6P338 4.3 41.7 1.0 CZ A:ARG276 4.3 31.7 1.0 NH1 A:ARG276 4.4 37.2 1.0 OE2 A:GLU97 4.5 36.3 1.0 CB A:ASP118 4.5 10.8 1.0 C2 A:F6P338 4.5 39.1 1.0 O3 A:F6P338 4.6 37.1 1.0 N A:GLY122 4.9 27.1 1.0 N A:ASP121 4.9 24.0 1.0 C A:ASP121 5.0 25.7 1.0

Manganese binding site 2 out of 2 in the The T-State Structure of Lys 42 to Ala Mutant of the Pig Kidney Fructose 1,6-Bisphosphatase Expressed in E. Coli


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of The T-State Structure of Lys 42 to Ala Mutant of the Pig Kidney Fructose 1,6-Bisphosphatase Expressed in E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn339 b:49.9 occ:1.00 O B:HOH342 1.9 51.8 1.0 OE2 B:GLU280 2.1 11.9 1.0 OD2 B:ASP118 2.4 17.5 1.0 OD1 B:ASP121 2.4 25.6 1.0 O1 B:F6P338 3.1 48.8 1.0 CG B:ASP118 3.3 12.0 1.0 CD B:GLU280 3.3 11.7 1.0 CG B:ASP121 3.6 26.9 1.0 OD1 B:ASP118 3.6 17.3 1.0 CB B:ASP121 4.1 22.8 1.0 CG B:GLU280 4.1 8.0 1.0 O B:HOH341 4.1 8.0 1.0 CA B:ASP121 4.2 21.0 1.0 OE1 B:GLU280 4.2 14.3 1.0 O2 B:F6P338 4.3 37.4 1.0 OE2 B:GLU97 4.3 38.1 1.0 C1 B:F6P338 4.3 40.7 1.0 CB B:ASP118 4.5 2.1 1.0 CG B:GLU97 4.6 29.5 1.0 O3 B:F6P338 4.6 39.3 1.0 OD2 B:ASP121 4.7 22.9 1.0 CD B:GLU97 4.7 33.1 1.0 C2 B:F6P338 4.7 36.2 1.0 N B:GLY122 4.7 28.9 1.0 C3 B:F6P338 4.9 33.4 1.0 O B:LEU120 5.0 3.7 1.0

G.Lu, B.Stec, E.L.Giroux, E.R.Kantrowitz. Evidence For An Active T-State Pig Kidney Fructose 1,6-Bisphosphatase: Interface Residue Lys-42 Is Important For Allosteric Inhibition and Amp Cooperativity. Protein Sci. V. 5 2333 1996.
ISSN: ISSN 0961-8368
PubMed: 8931152