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Magnesium in PDB 7key: Protein Tyrosine Phosphatase 1B, Apo

Enzymatic activity of Protein Tyrosine Phosphatase 1B, Apo

All present enzymatic activity of Protein Tyrosine Phosphatase 1B, Apo:
3.1.3.48;

Protein crystallography data

The structure of Protein Tyrosine Phosphatase 1B, Apo, PDB code: 7key was solved by K.P.Battaile, Y.Chirgadze, M.Ruzanov, V.Romanov, K.Lam, R.Gordon, A.Lin, R.Lam, E.Pai, N.Chirgadze, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 76.52 / 1.77
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.353, 88.353, 104.744, 90, 90, 120
R / Rfree (%) 19.9 / 20.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Protein Tyrosine Phosphatase 1B, Apo (pdb code 7key). 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, Apo, PDB code: 7key:

Magnesium binding site 1 out of 1 in 7key

Go back to Magnesium Binding Sites List in 7key
Magnesium binding site 1 out of 1 in the Protein Tyrosine Phosphatase 1B, Apo


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, Apo within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg904

b:43.5
occ:1.00
O A:HOH1005 2.0 46.5 1.0
O A:HOH1093 2.2 61.6 1.0
O A:HOH1032 2.2 39.7 1.0
OE1 A:GLU130 4.2 31.9 1.0
OE1 A:GLU129 4.4 27.4 1.0
O A:HOH1092 4.4 36.2 1.0
OE2 A:GLU130 4.4 38.2 1.0
O A:HOH1102 4.5 45.3 1.0
CD A:GLU130 4.7 35.3 1.0

Reference:

Y.N.Chirgadze, K.P.Battaile, I.V.Likhachev, N.K.Balabaev, R.D.Gordon, V.Romanov, A.Lin, R.Karisch, R.Lam, M.Ruzanov, E.V.Brazhnikov, E.F.Pai, B.G.Neel, N.Y.Chirgadze. Signal Transfer in Human Protein Tyrosine Phosphatase PTP1B From Allosteric Inhibitor P00058. J.Biomol.Struct.Dyn. 1 2021.
ISSN: ESSN 1538-0254
PubMed: 34705594
DOI: 10.1080/07391102.2021.1994879
Page generated: Wed Oct 2 22:15:21 2024

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