Phosphorus in PDB 1akc: 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: 1akc 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 / 2.30
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 69.800, 91.300, 127.800, 90.00, 90.00, 90.00
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 1akc). 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 Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue, PDB code: 1akc:

Phosphorus binding site 1 out of 1 in 1akc

Go back to Phosphorus Binding Sites List in 1akc
Phosphorus binding site 1 out of 1 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:24.6
occ:1.00
 P A:PPE411 0.0 24.6 1.0
OP1 A:PPE411 1.4 18.8 1.0
OP3 A:PPE411 1.5 21.2 1.0
OP2 A:PPE411 1.5 26.9 1.0
OP4 A:PPE411 1.6 19.1 1.0
C5A A:PPE411 2.6 28.5 1.0
OG A:SER107 3.5 33.6 1.0
NH2 A:ARG266 3.6 28.5 1.0
NH1 A:ARG266 3.7 25.7 1.0
N A:GLY108 3.8 25.6 1.0
OG1 A:THR109 3.9 28.2 1.0
CB A:SER107 3.9 49.5 1.0
N A:THR109 4.0 25.4 1.0
C5 A:PPE411 4.0 23.3 1.0
CZ A:ARG266 4.1 35.4 1.0
OG A:SER255 4.3 36.8 1.0
CA A:GLY108 4.3 26.6 1.0
C4A A:PPE411 4.3 11.7 1.0
CB A:ALA257 4.4 18.4 1.0
C4 A:PPE411 4.6 20.4 1.0
CB A:SER255 4.6 27.2 1.0
C A:GLY108 4.7 16.8 1.0
C A:SER107 4.8 32.3 1.0
CB A:THR109 4.8 22.2 1.0
OE2 A:PPE411 4.9 84.8 1.0
CA A:SER107 4.9 34.5 1.0
C6 A:PPE411 5.0 36.1 1.0
CA A:THR109 5.0 24.6 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 13:04:25 2020

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