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Chlorine in PDB 3nr8: Crystal Structure of Human SHIP2

Enzymatic activity of Crystal Structure of Human SHIP2

All present enzymatic activity of Crystal Structure of Human SHIP2:
3.1.3.1;

Protein crystallography data

The structure of Crystal Structure of Human SHIP2, PDB code: 3nr8 was solved by L.Tresaugues, M.Welin, C.H.Arrowsmith, H.Berglund, C.Bountra, R.Collins, A.M.Edwards, S.Flodin, A.Flores, S.Graslund, M.Hammarstrom, I.Johansson, T.Karlberg, S.Kol, T.Kotenyova, E.Kouznetsova, M.Moche, T.Nyman, C.Persson, H.Schuler, P.Schutz, M.I.Siponen, A.G.Thorsell, S.Van Derberg, E.Wahlberg, J.Weigelt, P.Nordlund, Structural Genomics Consortium(Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.796, 61.177, 114.320, 90.00, 91.90, 90.00
R / Rfree (%) 21.4 / 27.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human SHIP2 (pdb code 3nr8). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human SHIP2, PDB code: 3nr8:

Chlorine binding site 1 out of 1 in 3nr8

Go back to Chlorine Binding Sites List in 3nr8
Chlorine binding site 1 out of 1 in the Crystal Structure of Human SHIP2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human SHIP2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1

b:39.2
occ:1.00
O B:HOH36 3.1 42.9 1.0
OG B:SER564 3.6 41.7 1.0
NZ B:LYS541 3.9 44.4 1.0
CB B:SER564 4.4 39.6 1.0
CE B:LYS541 4.5 42.4 1.0
O B:HOH6 4.8 39.4 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: ISSN 0969-2126
PubMed: 24704254
DOI: 10.1016/J.STR.2014.01.013
Page generated: Sat Dec 12 09:58:02 2020

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