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Sodium in PDB 1mos: Isomerase Domain of Glucosamine 6-Phosphate Synthase Complexed with 2- Amino-2-Deoxyglucitol 6-Phosphate

Enzymatic activity of Isomerase Domain of Glucosamine 6-Phosphate Synthase Complexed with 2- Amino-2-Deoxyglucitol 6-Phosphate

All present enzymatic activity of Isomerase Domain of Glucosamine 6-Phosphate Synthase Complexed with 2- Amino-2-Deoxyglucitol 6-Phosphate:
2.6.1.16;

Protein crystallography data

The structure of Isomerase Domain of Glucosamine 6-Phosphate Synthase Complexed with 2- Amino-2-Deoxyglucitol 6-Phosphate, PDB code: 1mos was solved by A.Teplyakov, G.Obmolova, M.A.Badet-Denisot, B.Badet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.00 / 2.00
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 143.900, 143.900, 172.800, 90.00, 90.00, 120.00
R / Rfree (%) n/a / 28.7

Sodium Binding Sites:

The binding sites of Sodium atom in the Isomerase Domain of Glucosamine 6-Phosphate Synthase Complexed with 2- Amino-2-Deoxyglucitol 6-Phosphate (pdb code 1mos). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Isomerase Domain of Glucosamine 6-Phosphate Synthase Complexed with 2- Amino-2-Deoxyglucitol 6-Phosphate, PDB code: 1mos:

Sodium binding site 1 out of 1 in 1mos

Go back to Sodium Binding Sites List in 1mos
Sodium binding site 1 out of 1 in the Isomerase Domain of Glucosamine 6-Phosphate Synthase Complexed with 2- Amino-2-Deoxyglucitol 6-Phosphate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Isomerase Domain of Glucosamine 6-Phosphate Synthase Complexed with 2- Amino-2-Deoxyglucitol 6-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na614

b:44.4
occ:1.00
O3S A:MES610 2.4 48.9 1.0
O A:HOH26 2.5 33.3 1.0
O A:HOH22 2.5 32.0 1.0
O A:HOH73 2.6 40.7 1.0
O A:HOH23 2.7 32.0 1.0
S A:MES610 3.7 44.5 1.0
O A:HOH162 3.8 55.4 1.0
OD1 A:ASP474 3.8 30.8 1.0
CG A:ASP474 4.2 45.3 1.0
OD2 A:ASP474 4.2 28.6 1.0
O2S A:MES610 4.2 42.1 1.0
OE2 A:GLU569 4.2 44.5 1.0
C7 A:MES610 4.4 37.7 1.0
N A:ASP474 4.5 20.5 1.0
O A:HOH55 4.6 37.4 1.0
C8 A:MES610 4.6 42.3 1.0
O1S A:MES610 4.6 51.2 1.0
O A:ARG472 4.8 26.8 1.0
O A:HOH11 4.8 28.4 1.0
O A:HOH24 4.8 32.1 1.0
O A:HOH63 4.9 38.7 1.0
CA A:GLY473 4.9 24.3 1.0

Reference:

A.Teplyakov, G.Obmolova, M.A.Badet-Denisot, B.Badet. The Mechanism of Sugar Phosphate Isomerization By Glucosamine 6-Phosphate Synthase. Protein Sci. V. 8 596 1999.
ISSN: ISSN 0961-8368
PubMed: 10091662
Page generated: Sun Oct 6 20:34:09 2024

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