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Bromine in PDB 1qui: Phosphate-Binding Protein Mutant with Asp 137 Replaced By Gly Complex with Bromine and Phosphate

Protein crystallography data

The structure of Phosphate-Binding Protein Mutant with Asp 137 Replaced By Gly Complex with Bromine and Phosphate, PDB code: 1qui was solved by N.Yao, A.Choudhary, P.S.Ledvina, F.A.Quiocho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.970, 63.980, 123.970, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 21.8

Bromine Binding Sites:

The binding sites of Bromine atom in the Phosphate-Binding Protein Mutant with Asp 137 Replaced By Gly Complex with Bromine and Phosphate (pdb code 1qui). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Phosphate-Binding Protein Mutant with Asp 137 Replaced By Gly Complex with Bromine and Phosphate, PDB code: 1qui:

Bromine binding site 1 out of 1 in 1qui

Go back to Bromine Binding Sites List in 1qui
Bromine binding site 1 out of 1 in the Phosphate-Binding Protein Mutant with Asp 137 Replaced By Gly Complex with Bromine and Phosphate


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Phosphate-Binding Protein Mutant with Asp 137 Replaced By Gly Complex with Bromine and Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br323

b:29.5
occ:1.00
O A:HOH611 3.0 41.9 1.0
NE A:ARG135 3.2 4.1 1.0
N A:GLY137 3.2 19.2 1.0
O A:HOH585 3.3 35.2 1.0
N A:GLY176 3.3 3.9 1.0
NH2 A:ARG135 3.7 4.5 1.0
O A:GLY174 3.7 10.7 1.0
CA A:LYS175 3.8 8.5 1.0
CZ A:ARG135 3.9 8.4 1.0
N A:ALA136 3.9 12.8 1.0
CA A:GLY137 4.0 18.5 1.0
C A:LYS175 4.1 6.2 1.0
CD A:ARG135 4.2 5.6 1.0
C A:ALA136 4.2 19.0 1.0
CA A:GLY176 4.3 6.4 1.0
C A:GLY137 4.3 17.8 1.0
CB A:ARG135 4.3 3.8 1.0
O A:GLY137 4.3 19.9 1.0
CG A:LYS175 4.3 20.2 1.0
CA A:ALA136 4.4 16.2 1.0
CB A:ALA136 4.5 17.9 1.0
NZ A:LYS175 4.6 34.3 1.0
C A:ARG135 4.6 8.5 1.0
C A:GLY174 4.6 8.2 1.0
CB A:LYS175 4.7 13.3 1.0
CA A:ARG135 4.7 6.4 1.0
N A:LYS175 4.7 7.0 1.0
CG A:ARG135 4.8 3.0 1.0

Reference:

N.Yao, P.S.Ledvina, A.Choudhary, F.A.Quiocho. Modulation of A Salt Link Does Not Affect Binding of Phosphate to Its Specific Active Transport Receptor. Biochemistry V. 35 2079 1996.
ISSN: ISSN 0006-2960
PubMed: 8652549
DOI: 10.1021/BI952686R
Page generated: Wed Jul 10 17:14:57 2024

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