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Chlorine in PDB 2fvv: Human Diphosphoinositol Polyphosphate Phosphohydrolase 1

Enzymatic activity of Human Diphosphoinositol Polyphosphate Phosphohydrolase 1

All present enzymatic activity of Human Diphosphoinositol Polyphosphate Phosphohydrolase 1:
3.6.1.52;

Protein crystallography data

The structure of Human Diphosphoinositol Polyphosphate Phosphohydrolase 1, PDB code: 2fvv was solved by B.M.Hallberg, P.Kursula, D.Ogg, C.Arrowsmith, H.Berglund, A.Edwards, M.Ehn, S.Flodin, S.Graslund, M.Hammarstrom, M.Hogbom, L.Holmberg-Schiavone, T.Kotenyova, P.Nilsson-Ehle, P.Nordlund, T.Nyman, J.Sagemark, P.Stenmark, M.Sundstrom, A.G.Thorsell, S.Van Den Berg, J.Weigelt, C.Persson, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.653, 59.900, 61.735, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 20.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Human Diphosphoinositol Polyphosphate Phosphohydrolase 1 (pdb code 2fvv). 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 Human Diphosphoinositol Polyphosphate Phosphohydrolase 1, PDB code: 2fvv:

Chlorine binding site 1 out of 1 in 2fvv

Go back to Chlorine Binding Sites List in 2fvv
Chlorine binding site 1 out of 1 in the Human Diphosphoinositol Polyphosphate Phosphohydrolase 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Diphosphoinositol Polyphosphate Phosphohydrolase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2361

b:24.9
occ:1.00
O A:HOH4004 2.9 33.5 1.0
N A:GLU32 3.0 20.9 1.0
OG A:SER28 3.1 25.2 1.0
N A:SER28 3.2 18.4 1.0
N A:GLU33 3.3 16.3 1.0
OG A:SER30 3.5 24.8 0.5
N A:GLU31 3.6 21.4 1.0
O A:SER28 3.7 19.8 1.0
CA A:GLU32 3.8 21.5 1.0
CB A:ARG27 3.8 19.5 1.0
N A:ARG27 3.8 14.9 1.0
CB A:GLU32 3.9 23.3 1.0
O A:GLU33 3.9 16.4 1.0
CB A:SER28 3.9 20.4 1.0
C A:GLU31 3.9 20.7 1.0
C A:GLU32 3.9 19.4 1.0
CA A:SER28 3.9 19.9 1.0
CA A:GLU31 3.9 19.5 1.0
C A:ARG27 4.0 19.7 1.0
CA A:ARG27 4.1 17.6 1.0
C A:SER28 4.1 20.4 1.0
CA A:GLU33 4.2 16.3 0.2
CA A:GLU33 4.2 16.8 0.8
C A:SER30 4.3 25.2 1.0
CB A:GLU33 4.3 19.7 0.2
CB A:GLU33 4.3 17.0 0.8
CB A:SER30 4.5 27.0 0.5
C A:GLU33 4.6 13.5 1.0
N A:SER30 4.6 25.7 1.0
CB A:PHE26 4.6 15.7 1.0
CA A:SER30 4.7 26.3 0.5
CB A:SER30 4.7 28.8 0.5
C A:PHE26 4.7 14.2 1.0
O A:HOH4142 4.7 42.3 1.0
CA A:SER30 4.8 24.7 0.5
CG A:GLU33 4.9 28.0 0.8
CG A:GLU32 4.9 31.2 1.0
CG A:ARG27 5.0 32.4 1.0
O A:SER30 5.0 24.5 1.0

Reference:

A.G.Thorsell, C.Persson, S.Graslund, M.Hammarstrom, R.D.Busam, B.M.Hallberg. Crystal Structure of Human Diphosphoinositol Phosphatase 1 Proteins V. 77 242 2009.
ISSN: ISSN 0887-3585
PubMed: 19585659
DOI: 10.1002/PROT.22489
Page generated: Thu Jul 10 22:13:16 2025

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