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Magnesium in PDB 4cmn: Crystal Structure of Ocrl in Complex with A Phosphate Ion

Enzymatic activity of Crystal Structure of Ocrl in Complex with A Phosphate Ion

All present enzymatic activity of Crystal Structure of Ocrl in Complex with A Phosphate Ion:
3.1.3.36;

Protein crystallography data

The structure of Crystal Structure of Ocrl in Complex with A Phosphate Ion, PDB code: 4cmn was solved by L.Tresaugues, M.Moche, C.H.Arrowsmith, H.Berglund, C.Bountra, A.M.Edwards, T.Ekblad, S.Flodin, S.Graslund, T.Karlberg, 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) 48.922 / 3.13
Space group P 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 146.766, 146.766, 146.766, 90.00, 90.00, 90.00
R / Rfree (%) 20.96 / 26.28

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Ocrl in Complex with A Phosphate Ion (pdb code 4cmn). 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 Ocrl in Complex with A Phosphate Ion, PDB code: 4cmn:

Magnesium binding site 1 out of 1 in 4cmn

Go back to Magnesium Binding Sites List in 4cmn
Magnesium binding site 1 out of 1 in the Crystal Structure of Ocrl in Complex with A Phosphate Ion


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 Ocrl in Complex with A Phosphate Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1561

b:0.2
occ:1.00
OE1 A:GLU278 2.3 0.6 1.0
OD1 A:ASN250 2.7 0.1 1.0
O A:HOH2002 3.2 80.7 1.0
O2 A:PO41560 3.2 0.5 1.0
CD A:GLU278 3.3 0.4 1.0
O3 A:PO41560 3.4 0.4 1.0
OE2 A:GLU278 3.7 0.2 1.0
CD1 A:LEU281 3.8 93.0 1.0
CG A:ASN250 3.9 0.4 1.0
P A:PO41560 3.9 0.9 1.0
CD2 A:LEU281 4.3 91.5 1.0
CA A:ASN250 4.7 99.2 1.0
O1 A:PO41560 4.7 0.7 1.0
CG A:GLU278 4.7 0.4 1.0
CG A:LEU281 4.7 95.9 1.0
CB A:ASN250 4.8 95.8 1.0
ND2 A:ASN250 4.8 0.4 1.0
OD2 A:ASP523 4.8 0.1 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 Dec 14 11:41:24 2020

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