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Chlorine in PDB 1d2a: Crystal Structure of A Yeast Low Molecular Weight Protein Tyrosine Phosphatase (LTP1) Complexed with the Activator Adenine

Enzymatic activity of Crystal Structure of A Yeast Low Molecular Weight Protein Tyrosine Phosphatase (LTP1) Complexed with the Activator Adenine

All present enzymatic activity of Crystal Structure of A Yeast Low Molecular Weight Protein Tyrosine Phosphatase (LTP1) Complexed with the Activator Adenine:
3.1.3.48;

Protein crystallography data

The structure of Crystal Structure of A Yeast Low Molecular Weight Protein Tyrosine Phosphatase (LTP1) Complexed with the Activator Adenine, PDB code: 1d2a was solved by S.Wang, C.V.Stauffacher, R.L.Van Etten, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.492, 63.272, 97.590, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 24.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of A Yeast Low Molecular Weight Protein Tyrosine Phosphatase (LTP1) Complexed with the Activator Adenine (pdb code 1d2a). 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 A Yeast Low Molecular Weight Protein Tyrosine Phosphatase (LTP1) Complexed with the Activator Adenine, PDB code: 1d2a:

Chlorine binding site 1 out of 1 in 1d2a

Go back to Chlorine Binding Sites List in 1d2a
Chlorine binding site 1 out of 1 in the Crystal Structure of A Yeast Low Molecular Weight Protein Tyrosine Phosphatase (LTP1) Complexed with the Activator Adenine


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 A Yeast Low Molecular Weight Protein Tyrosine Phosphatase (LTP1) Complexed with the Activator Adenine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl404

b:13.9
occ:1.00
 OG1 A:THR48 2.9 14.8 1.0
ND2 A:ASN100 3.2 12.1 1.0
ND2 A:ASN97 3.2 9.7 1.0
O A:HOH413 3.3 13.6 1.0
CA A:ASN97 3.7 14.0 1.0
O A:ALA13 3.8 10.5 1.0
CD1 A:LEU14 3.8 11.0 1.0
CG2 A:THR48 3.8 10.5 1.0
CA A:LEU14 3.9 11.5 1.0
CB A:THR48 3.9 12.2 1.0
CB A:LEU14 3.9 15.8 1.0
CB A:ASN100 4.0 14.0 1.0
C A:ALA13 4.0 12.1 1.0
CG A:ASN100 4.0 19.7 1.0
N A:LEU14 4.1 14.0 1.0
O A:SER96 4.1 13.5 1.0
CG A:ASN97 4.2 16.4 1.0
N A:ASN97 4.3 16.9 1.0
CB A:ASN97 4.4 13.1 1.0
C A:SER96 4.5 14.6 1.0
CG A:LEU14 4.5 18.4 1.0
O A:ASN97 4.5 14.6 1.0
C A:ASN97 4.6 12.4 1.0
CA A:ALA13 4.9 15.8 1.0
OG A:SER96 4.9 10.3 1.0

Reference:

S.Wang, C.V.Stauffacher, R.L.Van Etten. Structural and Mechanistic Basis For the Activation of A Low-Molecular Weight Protein Tyrosine Phosphatase By Adenine. Biochemistry V. 39 1234 2000.
ISSN: ISSN 0006-2960
PubMed: 10684601
DOI: 10.1021/BI991515+
Page generated: Fri Jul 19 21:31:17 2024

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