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Chlorine in PDB 4ikc: Crystal Structure of Catalytic Domain of Ptprq

Enzymatic activity of Crystal Structure of Catalytic Domain of Ptprq

All present enzymatic activity of Crystal Structure of Catalytic Domain of Ptprq:
3.1.3.48;

Protein crystallography data

The structure of Crystal Structure of Catalytic Domain of Ptprq, PDB code: 4ikc was solved by K.R.Yu, S.E.Ryu, S.J.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.39 / 1.56
Space group P 64
Cell size a, b, c (Å), α, β, γ (°) 77.580, 77.580, 85.240, 90.00, 90.00, 120.00
R / Rfree (%) 14.7 / 16.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Catalytic Domain of Ptprq (pdb code 4ikc). 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 Catalytic Domain of Ptprq, PDB code: 4ikc:

Chlorine binding site 1 out of 1 in 4ikc

Go back to Chlorine Binding Sites List in 4ikc
Chlorine binding site 1 out of 1 in the Crystal Structure of Catalytic Domain of Ptprq


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 Catalytic Domain of Ptprq within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl3002

b:21.4
occ:1.00
HD1 A:HIS2878 2.3 15.8 1.0
HG1 A:THR2781 2.7 29.9 1.0
O A:HOH3226 2.8 26.6 1.0
HA3 A:GLY2756 2.8 15.0 1.0
HA A:SER2879 2.9 15.2 1.0
OG1 A:THR2781 2.9 24.9 1.0
ND1 A:HIS2878 3.1 13.2 1.0
HG22 A:THR2781 3.2 25.5 1.0
H A:GLY2756 3.3 15.4 1.0
C A:SER2879 3.4 13.1 1.0
CA A:SER2879 3.5 12.7 1.0
HG21 A:THR2781 3.5 25.5 1.0
CA A:GLY2756 3.6 12.5 1.0
HE1 A:HIS2878 3.6 18.4 1.0
O A:SER2879 3.6 12.7 1.0
O A:HOH3185 3.6 27.4 1.0
CG2 A:THR2781 3.7 21.2 1.0
HA A:SER2880 3.7 13.8 1.0
CE1 A:HIS2878 3.8 15.3 1.0
N A:SER2880 3.8 12.9 1.0
N A:GLY2756 3.8 12.8 1.0
HA2 A:GLY2756 3.8 15.0 1.0
CB A:THR2781 3.9 22.8 1.0
N A:SER2879 3.9 12.4 1.0
HG3 A:MET2779 4.1 21.4 1.0
HE2 A:MET2779 4.1 30.4 1.0
H A:SER2880 4.1 15.5 1.0
C A:HIS2878 4.2 11.9 1.0
H A:SER2879 4.3 14.9 1.0
HB2 A:HIS2878 4.3 13.8 1.0
CG A:HIS2878 4.3 11.6 1.0
CA A:SER2880 4.3 11.5 1.0
O A:HIS2878 4.3 12.5 1.0
HB A:THR2781 4.4 27.4 1.0
SG A:CYS2791 4.5 68.3 1.0
O A:HOH3154 4.5 21.0 1.0
H A:THR2781 4.6 23.9 1.0
HG23 A:THR2781 4.6 25.5 1.0
H A:LEU2780 4.7 18.6 1.0
CB A:HIS2878 4.7 11.6 1.0
CB A:SER2879 4.9 13.0 1.0
C A:GLY2756 4.9 14.2 1.0
HB2 A:SER2880 4.9 17.3 1.0
N A:THR2781 5.0 19.9 1.0
HB2 A:SER2879 5.0 15.6 1.0
CG A:MET2779 5.0 17.9 1.0

Reference:

K.R.Yu, Y.J.Kim, S.K.Jung, B.Ku, H.Park, S.Y.Cho, H.Jung, S.J.Chung, K.H.Bae, S.C.Lee, B.Y.Kim, R.L.Erikson, S.E.Ryu, S.J.Kim. Structural Basis For the Dephosphorylating Activity of Ptprq Towards Phosphatidylinositide Substrates Acta Crystallogr.,Sect.D V. 69 1522 2013.
ISSN: ISSN 0907-4449
PubMed: 23897475
DOI: 10.1107/S0907444913010457
Page generated: Sat Dec 12 10:46:04 2020

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