Phosphorus in PDB 1aam: The Structural Basis For the Altered Substrate Specificity of the R292D Active Site Mutant of Aspartate Aminotransferase From E. Coli

Enzymatic activity of The Structural Basis For the Altered Substrate Specificity of the R292D Active Site Mutant of Aspartate Aminotransferase From E. Coli

All present enzymatic activity of The Structural Basis For the Altered Substrate Specificity of the R292D Active Site Mutant of Aspartate Aminotransferase From E. Coli:
2.6.1.1;

Protein crystallography data

The structure of The Structural Basis For the Altered Substrate Specificity of the R292D Active Site Mutant of Aspartate Aminotransferase From E. Coli, PDB code: 1aam was solved by S.C.Almo, D.L.Smith, A.T.Danishefsky, D.Ringe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 155.400, 87.000, 80.100, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the The Structural Basis For the Altered Substrate Specificity of the R292D Active Site Mutant of Aspartate Aminotransferase From E. Coli (pdb code 1aam). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total only one binding site of Phosphorus was determined in the The Structural Basis For the Altered Substrate Specificity of the R292D Active Site Mutant of Aspartate Aminotransferase From E. Coli, PDB code: 1aam:

Phosphorus binding site 1 out of 1 in 1aam

Go back to Phosphorus Binding Sites List in 1aam
Phosphorus binding site 1 out of 1 in the The Structural Basis For the Altered Substrate Specificity of the R292D Active Site Mutant of Aspartate Aminotransferase From E. Coli


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of The Structural Basis For the Altered Substrate Specificity of the R292D Active Site Mutant of Aspartate Aminotransferase From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P409

b:15.0
occ:1.00
 P A:PLP409 0.0 15.0 1.0
O1P A:PLP409 1.5 15.0 1.0
O2P A:PLP409 1.5 15.0 1.0
O3P A:PLP409 1.6 15.0 1.0
O4P A:PLP409 1.6 15.0 1.0
C5A A:PLP409 2.5 15.0 1.0
O A:GLY114 3.3 15.0 1.0
CG2 A:THR116 3.3 15.0 1.0
CB A:THR116 3.6 15.0 1.0
C5 A:PLP409 3.9 15.0 1.0
NH1 A:ARG266 4.1 15.0 1.0
N A:THR116 4.2 15.0 1.0
C4A A:PLP409 4.2 15.0 1.0
NZ A:LYS258 4.3 15.0 1.0
NH2 A:ARG266 4.3 15.0 1.0
C A:GLY114 4.4 15.0 1.0
CA A:THR116 4.4 15.0 1.0
CE A:LYS258 4.4 15.0 1.0
OG A:SER255 4.5 15.0 1.0
C4 A:PLP409 4.6 15.0 1.0
CZ A:ARG266 4.7 15.0 1.0
OG1 A:THR116 4.8 15.0 1.0
CA A:GLY114 4.8 15.0 1.0
C6 A:PLP409 4.9 15.0 1.0
C A:GLY115 4.9 15.0 1.0
OG A:SER257 4.9 15.0 1.0
CB A:SER257 5.0 15.0 1.0

Reference:

S.C.Almo, D.L.Smith, A.T.Danishefsky, D.Ringe. The Structural Basis For the Altered Substrate Specificity of the R292D Active Site Mutant of Aspartate Aminotransferase From E. Coli. Protein Eng. V. 7 405 1994.
ISSN: ISSN 0269-2139
PubMed: 7909946
DOI: 10.1093/PROTEIN/7.3.405
Page generated: Fri Sep 25 12:41:43 2020

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