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Magnesium in PDB 2hwg: Structure of Phosphorylated Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System

Enzymatic activity of Structure of Phosphorylated Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System

All present enzymatic activity of Structure of Phosphorylated Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System:
2.7.3.9;

Protein crystallography data

The structure of Structure of Phosphorylated Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System, PDB code: 2hwg was solved by K.Lim, A.Teplyakov, O.Herzberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 85.487, 94.084, 161.007, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 28.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Phosphorylated Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System (pdb code 2hwg). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Phosphorylated Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System, PDB code: 2hwg:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2hwg

Go back to Magnesium Binding Sites List in 2hwg
Magnesium binding site 1 out of 2 in the Structure of Phosphorylated Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Phosphorylated Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg901

b:21.9
occ:1.00
O A:HOH1001 1.9 32.4 1.0
O2P A:NEP189 2.0 20.6 1.0
OE1 A:GLU431 2.0 9.2 1.0
OD2 A:ASP455 2.1 13.7 1.0
O2 A:OXL903 2.2 19.6 1.0
O1 A:OXL903 2.2 19.5 1.0
C2 A:OXL903 2.9 21.1 1.0
C1 A:OXL903 2.9 20.8 1.0
CD A:GLU431 3.0 11.3 1.0
P A:NEP189 3.1 21.5 1.0
CG A:ASP455 3.2 13.7 1.0
O1P A:NEP189 3.5 21.2 1.0
OE2 A:GLU431 3.5 13.3 1.0
NH2 A:ARG358 3.6 14.9 1.0
CB A:ASP455 3.8 14.5 1.0
O3P A:NEP189 3.8 21.4 1.0
NH1 A:ARG332 3.9 17.4 1.0
NH1 A:ARG465 3.9 11.1 1.0
O4 A:OXL903 4.1 23.1 1.0
O3 A:OXL903 4.1 18.6 1.0
OD1 A:ASP455 4.1 10.7 1.0
OD2 A:ASP335 4.2 15.3 1.0
CG A:GLU431 4.3 9.4 1.0
NE2 A:NEP189 4.4 22.2 1.0
N A:ASP455 4.6 14.1 1.0
CB A:GLU431 4.6 11.7 1.0
CZ A:ARG358 4.6 13.3 1.0
CE1 A:NEP189 4.6 22.9 1.0
CE A:MSE429 4.7 16.4 1.0
CZ A:ARG332 4.7 18.4 1.0
NH2 A:ARG332 4.8 16.4 1.0
CA A:ASP455 4.8 14.5 1.0
CZ A:ARG465 4.9 9.3 1.0
NH1 A:ARG358 4.9 14.9 1.0

Magnesium binding site 2 out of 2 in 2hwg

Go back to Magnesium Binding Sites List in 2hwg
Magnesium binding site 2 out of 2 in the Structure of Phosphorylated Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Phosphorylated Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg902

b:25.8
occ:1.00
OD2 B:ASP455 1.9 11.9 1.0
O B:HOH1002 1.9 17.1 1.0
OE1 B:GLU431 2.0 12.6 1.0
O1 B:OXL904 2.0 29.5 1.0
O2P B:NEP189 2.1 15.3 1.0
O2 B:OXL904 2.3 29.5 1.0
C1 B:OXL904 2.9 29.9 1.0
C2 B:OXL904 3.0 29.7 1.0
CG B:ASP455 3.0 11.7 1.0
CD B:GLU431 3.1 13.3 1.0
P B:NEP189 3.2 16.4 1.0
NH2 B:ARG465 3.4 20.2 1.0
OE2 B:GLU431 3.6 14.5 1.0
NH2 B:ARG358 3.6 17.2 1.0
O3P B:NEP189 3.7 15.0 1.0
CB B:ASP455 3.8 12.1 1.0
O1P B:NEP189 3.8 9.7 1.0
OD1 B:ASP455 4.0 7.5 1.0
OD2 B:ASP335 4.0 13.9 1.0
NH1 B:ARG332 4.1 20.8 1.0
O3 B:OXL904 4.1 27.0 1.0
O4 B:OXL904 4.2 30.6 1.0
CG B:GLU431 4.4 13.0 1.0
CE B:MSE429 4.4 18.6 1.0
CZ B:ARG358 4.5 15.7 1.0
N B:ASP455 4.5 14.1 1.0
CB B:GLU431 4.6 14.6 1.0
NE2 B:NEP189 4.6 13.8 1.0
CZ B:ARG465 4.7 16.9 1.0
NH2 B:ARG332 4.7 20.6 1.0
CE1 B:NEP189 4.7 11.8 1.0
CZ B:ARG332 4.8 19.4 1.0
CA B:ASP455 4.8 13.1 1.0
NH1 B:ARG358 4.9 12.5 1.0

Reference:

A.Teplyakov, K.Lim, P.P.Zhu, G.Kapadia, C.C.Chen, J.Schwartz, A.Howard, P.T.Reddy, A.Peterkofsky, O.Herzberg. Structure of Phosphorylated Enzyme I, the Phosphoenolpyruvate:Sugar Phosphotransferase System Sugar Translocation Signal Protein. Proc.Natl.Acad.Sci.Usa V. 103 16218 2006.
ISSN: ISSN 0027-8424
PubMed: 17053069
DOI: 10.1073/PNAS.0607587103
Page generated: Wed Aug 14 00:00:48 2024

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