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

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

All present enzymatic activity of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the 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 the Pyridoxal-5'-Phosphate Binding Lysine Residue, PDB code: 1aia was solved by J.Jaeger, J.N.Jansonius, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 86.900, 79.800, 89.900, 90.00, 118.90, 90.00
R / Rfree (%) 21 / n/a

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal-5'-Phosphate Binding Lysine Residue (pdb code 1aia). 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 the Pyridoxal-5'-Phosphate Binding Lysine Residue, PDB code: 1aia:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in 1aia

Go back to Phosphorus Binding Sites List in 1aia
Phosphorus binding site 1 out of 2 in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the 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 the Pyridoxal-5'-Phosphate Binding Lysine Residue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P411

b:17.6
occ:1.00
 P A:PMP411 0.0 17.6 1.0
O1P A:PMP411 1.5 10.2 1.0
O3P A:PMP411 1.5 16.6 1.0
O2P A:PMP411 1.5 18.4 1.0
O4P A:PMP411 1.6 18.0 1.0
C5A A:PMP411 2.4 19.5 1.0
OG A:SER255 3.6 17.0 1.0
NH2 A:ARG266 3.6 23.4 1.0
N A:GLY108 3.6 7.5 1.0
OG A:SER257 3.8 8.8 1.0
N A:THR109 3.8 13.0 1.0
C5 A:PMP411 3.9 21.8 1.0
OG1 A:THR109 3.9 15.0 1.0
N4A A:PMP411 4.0 30.7 1.0
OH B:TYR70 4.0 15.8 1.0
NH1 A:ARG266 4.1 10.4 1.0
CA A:GLY108 4.1 7.8 1.0
C4A A:PMP411 4.2 26.1 1.0
CZ A:ARG266 4.3 14.5 1.0
CB A:SER257 4.4 8.3 1.0
C A:GLY108 4.4 11.7 1.0
CB A:SER255 4.4 13.8 1.0
C A:GLY107 4.5 15.5 1.0
C4 A:PMP411 4.6 24.9 1.0
CA A:GLY107 4.6 13.9 1.0
C6 A:PMP411 4.8 16.6 1.0
CB A:THR109 4.9 13.4 1.0
CA A:THR109 4.9 15.2 1.0

Phosphorus binding site 2 out of 2 in 1aia

Go back to Phosphorus Binding Sites List in 1aia
Phosphorus binding site 2 out of 2 in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the 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 the Pyridoxal-5'-Phosphate Binding Lysine Residue within 5.0Å range:
probe atom residue distance (Å) B Occ
B:P411

b:20.4
occ:1.00
 P B:PMP411 0.0 20.4 1.0
O3P B:PMP411 1.5 27.5 1.0
O1P B:PMP411 1.5 20.8 1.0
O2P B:PMP411 1.5 13.8 1.0
O4P B:PMP411 1.6 13.1 1.0
C5A B:PMP411 2.5 17.0 1.0
NH2 B:ARG266 3.5 23.1 1.0
N B:GLY108 3.5 14.9 1.0
OG B:SER257 3.7 12.8 1.0
N B:THR109 3.8 18.0 1.0
OG B:SER255 3.8 13.1 1.0
C5 B:PMP411 3.9 18.7 1.0
OG1 B:THR109 4.0 17.3 1.0
OH A:TYR70 4.0 13.5 1.0
CA B:GLY108 4.0 13.9 1.0
NH1 B:ARG266 4.1 11.0 1.0
N4A B:PMP411 4.1 32.4 1.0
CZ B:ARG266 4.2 14.9 1.0
C4A B:PMP411 4.3 27.8 1.0
CB B:SER257 4.3 8.8 1.0
C B:GLY108 4.4 11.8 1.0
C B:GLY107 4.4 10.0 1.0
CB B:SER255 4.5 9.0 1.0
C4 B:PMP411 4.6 23.7 1.0
CA B:GLY107 4.6 7.0 1.0
C6 B:PMP411 4.8 13.7 1.0
CE1 A:TYR70 4.9 11.5 1.0
CA B:THR109 4.9 22.6 1.0
CB B:THR109 4.9 15.8 1.0
CZ A:TYR70 4.9 9.4 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 12:58:44 2020

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