Phosphorus in PDB 1aka: Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue

Enzymatic activity of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue

All present enzymatic activity of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue:
2.6.1.1;

Protein crystallography data

The structure of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue, PDB code: 1aka was solved by V.N.Malashkevich, J.N.Jansonius, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.10
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 55.870, 58.800, 75.810, 85.26, 108.96, 115.57
R / Rfree (%) n/a / n/a

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue (pdb code 1aka). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue, PDB code: 1aka:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in 1aka

Go back to Phosphorus Binding Sites List in 1aka
Phosphorus binding site 1 out of 2 in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P411

b:15.9
occ:1.00
 P A:PLP411 0.0 15.9 1.0
O1P A:PLP411 1.5 18.8 1.0
O2P A:PLP411 1.5 22.6 1.0
O3P A:PLP411 1.5 7.5 1.0
O4P A:PLP411 1.6 17.1 1.0
C5A A:PLP411 2.5 43.8 1.0
OG A:SER107 3.4 16.4 1.0
N A:GLY108 3.7 5.0 1.0
CB A:SER107 3.7 9.4 1.0
OG1 A:THR109 3.7 12.4 1.0
NH2 A:ARG266 3.7 10.2 1.0
O B:HOH419 3.8 47.1 1.0
N A:THR109 3.9 7.4 1.0
NH1 A:ARG266 3.9 18.3 1.0
C5 A:PLP411 4.0 45.6 1.0
OH B:TYR70 4.0 14.1 1.0
O4A A:PLP411 4.1 59.5 1.0
OG A:SER255 4.2 6.9 1.0
CA A:GLY108 4.2 3.6 1.0
CZ A:ARG266 4.3 16.3 1.0
CB A:ALA257 4.5 6.7 1.0
CE1 B:TYR70 4.5 4.7 1.0
C4A A:PLP411 4.5 39.3 1.0
C A:GLY108 4.6 4.7 1.0
C A:SER107 4.7 7.7 1.0
CB A:THR109 4.7 11.4 1.0
C4 A:PLP411 4.7 46.4 1.0
CZ B:TYR70 4.8 16.9 1.0
CA A:SER107 4.8 7.0 1.0
CA A:THR109 4.8 6.6 1.0
CB A:SER255 4.9 4.3 1.0
C6 A:PLP411 4.9 50.9 1.0

Phosphorus binding site 2 out of 2 in 1aka

Go back to Phosphorus Binding Sites List in 1aka
Phosphorus binding site 2 out of 2 in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue within 5.0Å range:
probe atom residue distance (Å) B Occ
B:P411

b:13.1
occ:1.00
 P B:PO4411 0.0 13.1 1.0
O1 B:PO4411 1.5 14.6 1.0
O3 B:PO4411 1.5 20.5 1.0
O2 B:PO4411 1.5 9.8 1.0
O4 B:PO4411 1.6 20.9 1.0
OG B:SER107 3.5 5.1 1.0
NH2 B:ARG266 3.6 10.8 1.0
O A:HOH604 3.7 24.9 1.0
NH1 B:ARG266 3.8 12.1 1.0
N B:GLY108 3.8 12.3 1.0
N B:THR109 3.8 8.1 1.0
OH A:TYR70 3.8 19.9 1.0
OG1 B:THR109 3.8 14.1 1.0
CB B:SER107 4.0 2.0 1.0
CA B:GLY108 4.1 3.4 1.0
CZ B:ARG266 4.1 17.4 1.0
OG B:SER255 4.2 18.3 1.0
CB B:ALA257 4.4 8.0 1.0
CE1 A:TYR70 4.5 13.4 1.0
C B:GLY108 4.5 8.7 1.0
CZ A:TYR70 4.6 22.0 1.0
CB B:SER255 4.8 15.1 1.0
C B:SER107 4.8 8.2 1.0
O B:HOH733 4.8 25.5 1.0
CB B:THR109 4.8 10.5 1.0
CA B:THR109 4.9 5.4 1.0
O B:HOH736 4.9 31.3 1.0
CA B:SER107 5.0 3.8 1.0

Reference:

V.N.Malashkevich, J.Jager, M.Ziak, U.Sauder, H.Gehring, P.Christen, J.N.Jansonius. Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal 5'-Phosphate-Binding Lysine Residue. Biochemistry V. 34 405 1995.
ISSN: ISSN 0006-2960
PubMed: 7819232
DOI: 10.1021/BI00002A004
Page generated: Fri Sep 25 13:03:57 2020

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