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Magnesium in PDB 4cml: Crystal Structure of INPP5B in Complex with Phosphatidylinositol 3,4-Bisphosphate

Enzymatic activity of Crystal Structure of INPP5B in Complex with Phosphatidylinositol 3,4-Bisphosphate

All present enzymatic activity of Crystal Structure of INPP5B in Complex with Phosphatidylinositol 3,4-Bisphosphate:
3.1.3.36;

Protein crystallography data

The structure of Crystal Structure of INPP5B in Complex with Phosphatidylinositol 3,4-Bisphosphate, PDB code: 4cml was solved by L.Tresaugues, C.H.Arrowsmith, H.Berglund, C.Bountra, A.M.Edwards, T.Ekblad, S.Flodin, S.Graslund, T.Karlberg, M.Moche, T.Nyman, H.Schuler, C.Silvander, A.G.Thorsell, J.Weigelt, M.Welin, P.Nordlund, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.50 / 2.30
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 133.661, 133.661, 133.661, 90.00, 90.00, 90.00
R / Rfree (%) 17.506 / 19.93

Other elements in 4cml:

The structure of Crystal Structure of INPP5B in Complex with Phosphatidylinositol 3,4-Bisphosphate also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of INPP5B in Complex with Phosphatidylinositol 3,4-Bisphosphate (pdb code 4cml). 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 Crystal Structure of INPP5B in Complex with Phosphatidylinositol 3,4-Bisphosphate, PDB code: 4cml:

Magnesium binding site 1 out of 1 in 4cml

Go back to Magnesium Binding Sites List in 4cml
Magnesium binding site 1 out of 1 in the Crystal Structure of INPP5B in Complex with Phosphatidylinositol 3,4-Bisphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of INPP5B in Complex with Phosphatidylinositol 3,4-Bisphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1569

b:40.0
occ:1.00
 O A:HOH2050 2.3 41.7 1.0
OE1 A:GLU303 2.4 28.5 1.0
OD1 A:ASN275 2.4 27.7 1.0
O A:HOH2018 2.4 26.7 1.0
O A:HOH2020 2.5 31.4 1.0
O A:HOH2023 2.5 41.5 1.0
CD A:GLU303 3.3 27.7 1.0
CG A:ASN275 3.4 27.7 1.0
OE2 A:GLU303 3.5 31.5 1.0
O A:HOH2022 3.7 51.1 1.0
O A:HOH2021 3.7 51.0 1.0
CA A:ASN275 3.9 25.1 1.0
OD2 A:ASP548 3.9 35.4 1.0
O A:HOH2305 4.0 34.4 1.0
CB A:ASN275 4.0 25.8 1.0
CD1 A:LEU306 4.2 27.0 1.0
OD1 A:ASP548 4.3 27.8 1.0
ND2 A:ASN275 4.5 26.6 1.0
CG A:ASP548 4.5 31.6 1.0
OD1 A:ASN273 4.6 24.6 1.0
C A:ASN275 4.7 25.4 1.0
CG A:GLU303 4.7 25.7 1.0
O5 A:52N1568 4.8 52.7 1.0
N A:ASN275 4.9 24.0 1.0
O A:ASN275 5.0 26.4 1.0

Reference:

L.Tresaugues, C.Silvander, S.Flodin, M.Welin, T.Nyman, S.Graslund, M.Hammarstrom, H.Berglund, P.Nordlund. Structural Basis For Phosphoinositide Substrate Recognition, Catalysis, and Membrane Interactions in Human Inositol Polyphosphate 5-Phosphatases. Structure V. 22 744 2014.
ISSN: ESSN 1878-4186
PubMed: 24704254
DOI: 10.1016/J.STR.2014.01.013
Page generated: Mon Aug 11 07:16:25 2025

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