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Sodium in PDB 3js5: Crystal Structure of Protein Tyrosine Phosphatase From Entamoeba Histolytica with Hepes in the Active Site. High Resolution, Alternative Crystal Form with 1 Molecule in Asymmetric Unit

Protein crystallography data

The structure of Crystal Structure of Protein Tyrosine Phosphatase From Entamoeba Histolytica with Hepes in the Active Site. High Resolution, Alternative Crystal Form with 1 Molecule in Asymmetric Unit, PDB code: 3js5 was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.24 / 1.94
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.433, 60.195, 72.229, 90.00, 90.00, 90.00
R / Rfree (%) 16.7 / 21.2

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Protein Tyrosine Phosphatase From Entamoeba Histolytica with Hepes in the Active Site. High Resolution, Alternative Crystal Form with 1 Molecule in Asymmetric Unit (pdb code 3js5). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Protein Tyrosine Phosphatase From Entamoeba Histolytica with Hepes in the Active Site. High Resolution, Alternative Crystal Form with 1 Molecule in Asymmetric Unit, PDB code: 3js5:

Sodium binding site 1 out of 1 in 3js5

Go back to Sodium Binding Sites List in 3js5
Sodium binding site 1 out of 1 in the Crystal Structure of Protein Tyrosine Phosphatase From Entamoeba Histolytica with Hepes in the Active Site. High Resolution, Alternative Crystal Form with 1 Molecule in Asymmetric Unit


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Protein Tyrosine Phosphatase From Entamoeba Histolytica with Hepes in the Active Site. High Resolution, Alternative Crystal Form with 1 Molecule in Asymmetric Unit within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na200

b:23.6
occ:1.00
O A:HOH311 2.3 11.1 1.0
O A:HOH310 2.3 8.5 1.0
O A:HOH165 2.4 12.2 1.0
O A:HOH183 2.4 11.8 1.0
O A:ILE68 2.5 12.8 1.0
O A:HOH172 3.6 13.5 1.0
C A:ILE68 3.6 13.3 1.0
CG A:ARG70 4.0 14.3 1.0
N A:ILE68 4.0 14.3 1.0
CB A:ARG70 4.1 13.8 1.0
CD A:ARG70 4.1 15.2 1.0
CA A:ILE68 4.3 14.1 1.0
CB A:ILE68 4.4 14.3 1.0
OD1 A:ASN10 4.4 12.3 1.0
OD1 A:ASP37 4.5 10.9 1.0
O A:SER38 4.5 12.0 1.0
N A:ARG70 4.5 13.4 1.0
O A:HOH246 4.5 26.9 1.0
O A:HOH179 4.6 10.7 1.0
C A:SER69 4.6 12.9 1.0
N A:SER69 4.7 12.9 1.0
NE A:ARG70 4.7 14.3 1.0
CA A:ARG70 4.9 13.7 1.0
CA A:SER69 5.0 12.9 1.0
O A:SER69 5.0 12.9 1.0

Reference:

A.S.Linford, N.M.Jiang, T.E.Edwards, N.E.Sherman, W.C.Van Voorhis, L.J.Stewart, P.J.Myler, B.L.Staker, W.A.Petri. Crystal Structure and Putative Substrate Identification For the Entamoeba Histolytica Low Molecular Weight Tyrosine Phosphatase. Mol.Biochem.Parasitol. V. 193 33 2014.
ISSN: ISSN 0166-6851
PubMed: 24548880
DOI: 10.1016/J.MOLBIOPARA.2014.01.003
Page generated: Sun Aug 17 15:53:49 2025

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