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Magnesium in PDB 7s4f: Protein Tyrosine Phosphatase 1B - F182Q Mutant Bound with Hepes

Enzymatic activity of Protein Tyrosine Phosphatase 1B - F182Q Mutant Bound with Hepes

All present enzymatic activity of Protein Tyrosine Phosphatase 1B - F182Q Mutant Bound with Hepes:
3.1.3.48;

Protein crystallography data

The structure of Protein Tyrosine Phosphatase 1B - F182Q Mutant Bound with Hepes, PDB code: 7s4f was solved by T.A.S.Brandao, A.C.Hengge, S.J.Johnson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.89 / 1.65
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.316, 88.316, 103.895, 90, 90, 120
R / Rfree (%) 18 / 20.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Protein Tyrosine Phosphatase 1B - F182Q Mutant Bound with Hepes (pdb code 7s4f). 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 Protein Tyrosine Phosphatase 1B - F182Q Mutant Bound with Hepes, PDB code: 7s4f:

Magnesium binding site 1 out of 1 in 7s4f

Go back to Magnesium Binding Sites List in 7s4f
Magnesium binding site 1 out of 1 in the Protein Tyrosine Phosphatase 1B - F182Q Mutant Bound with Hepes


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Protein Tyrosine Phosphatase 1B - F182Q Mutant Bound with Hepes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg304

b:32.8
occ:1.00
O A:HOH455 2.3 35.0 1.0
O A:HOH403 2.4 37.4 1.0
O A:HOH681 2.4 46.7 1.0
OE2 A:GLU130 4.2 24.2 1.0
O A:HOH697 4.3 42.7 1.0
OE1 A:GLU130 4.3 29.9 1.0
OE1 A:GLU129 4.4 23.1 1.0
O A:HOH523 4.4 53.7 1.0
O A:HOH651 4.5 40.4 1.0
NZ A:LYS128 4.6 68.2 1.0
CD A:GLU130 4.7 31.6 1.0

Reference:

R.Shen, R.M.Crean, K.J.Olsen, M.Corbella, A.R.Calixto, T.Richan, T.A.S.Brandao, R.D.Berry, A.Tolman, J.P.Loria, S.J.Johnson, S.C.L.Kamerlin, A.C.Hengge. Insights Into the Importance of Wpd-Loop Sequence For Activity and Structure in Protein Tyrosine Phosphatases. Chem Sci V. 13 13524 2022.
ISSN: ISSN 2041-6520
PubMed: 36507179
DOI: 10.1039/D2SC04135A
Page generated: Thu Oct 3 08:10:33 2024

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