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Zinc in PDB 2fkf: Phosphomannomutase/Phosphoglucomutase From Pseudomonas Aeruginosa with Alpha-D-Glucose 1,6-Bisphosphate Bound

Enzymatic activity of Phosphomannomutase/Phosphoglucomutase From Pseudomonas Aeruginosa with Alpha-D-Glucose 1,6-Bisphosphate Bound

All present enzymatic activity of Phosphomannomutase/Phosphoglucomutase From Pseudomonas Aeruginosa with Alpha-D-Glucose 1,6-Bisphosphate Bound:
5.4.2.2; 5.4.2.8;

Protein crystallography data

The structure of Phosphomannomutase/Phosphoglucomutase From Pseudomonas Aeruginosa with Alpha-D-Glucose 1,6-Bisphosphate Bound, PDB code: 2fkf was solved by C.A.Regni, L.J.Beamer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.865, 72.849, 91.258, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 24

Zinc Binding Sites:

The binding sites of Zinc atom in the Phosphomannomutase/Phosphoglucomutase From Pseudomonas Aeruginosa with Alpha-D-Glucose 1,6-Bisphosphate Bound (pdb code 2fkf). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Phosphomannomutase/Phosphoglucomutase From Pseudomonas Aeruginosa with Alpha-D-Glucose 1,6-Bisphosphate Bound, PDB code: 2fkf:

Zinc binding site 1 out of 1 in 2fkf

Go back to Zinc Binding Sites List in 2fkf
Zinc binding site 1 out of 1 in the Phosphomannomutase/Phosphoglucomutase From Pseudomonas Aeruginosa with Alpha-D-Glucose 1,6-Bisphosphate Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Phosphomannomutase/Phosphoglucomutase From Pseudomonas Aeruginosa with Alpha-D-Glucose 1,6-Bisphosphate Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:26.5
occ:1.00
 O3P A:SEP108 1.8 43.6 1.0
OD1 A:ASP246 1.9 34.0 1.0
OD2 A:ASP242 1.9 28.6 1.0
OD1 A:ASP244 2.0 34.7 1.0
CG A:ASP246 2.9 34.8 1.0
CG A:ASP244 2.9 33.3 1.0
CG A:ASP242 2.9 34.1 1.0
P A:SEP108 3.1 42.8 1.0
OD2 A:ASP244 3.1 33.4 1.0
OD1 A:ASP242 3.2 34.5 1.0
OD2 A:ASP246 3.2 35.4 1.0
OG A:SEP108 3.2 41.8 1.0
NZ A:LYS118 3.9 36.3 1.0
O1P A:SEP108 4.0 48.6 1.0
CB A:SEP108 4.1 40.3 1.0
NE A:ARG247 4.1 48.7 1.0
N A:ASP246 4.2 34.0 1.0
CG A:ARG247 4.2 39.6 1.0
O2P A:SEP108 4.2 45.9 1.0
CB A:ASP246 4.2 34.5 1.0
CB A:ASP242 4.2 33.7 1.0
CB A:ASP244 4.3 32.9 1.0
NE2 A:HIS329 4.3 39.6 1.0
CA A:SEP108 4.4 40.2 1.0
N A:ARG247 4.4 35.9 1.0
N A:ASP244 4.5 32.3 1.0
CA A:ASP246 4.5 34.7 1.0
CD A:ARG247 4.6 41.6 1.0
N A:GLY245 4.7 32.7 1.0
C A:ASP246 4.7 35.4 1.0
CA A:ASP244 4.7 32.7 1.0
CB A:ARG247 4.7 36.0 1.0
C A:ASP244 4.8 32.6 1.0
C A:SEP108 4.8 40.7 1.0
CE1 A:HIS329 5.0 41.3 1.0
NH2 A:ARG247 5.0 51.0 1.0

Reference:

C.Regni, A.M.Schramm, L.J.Beamer. The Reaction of Phosphohexomutase From Pseudomonas Aeruginosa: Structural Insights Into A Simple Processive Enzyme. J.Biol.Chem. V. 281 15564 2006.
ISSN: ISSN 0021-9258
PubMed: 16595672
DOI: 10.1074/JBC.M600590200
Page generated: Wed Oct 16 23:47:51 2024

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