Phosphorus in PDB 1ahx: Aspartate Aminotransferase Hexamutant

All present enzymatic activity of Aspartate Aminotransferase Hexamutant:
2.6.1.1;

The structure of Aspartate Aminotransferase Hexamutant, PDB code: 1ahx 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)	8.00 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	84.980, 78.690, 89.280, 90.00, 118.32, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Phosphorus atom in the Aspartate Aminotransferase Hexamutant (pdb code 1ahx). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the Aspartate Aminotransferase Hexamutant, PDB code: 1ahx:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in the Aspartate Aminotransferase Hexamutant


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Aspartate Aminotransferase Hexamutant within 5.0Å range: probe atom residue distance (Å) B Occ A:P410 b:18.8 occ:1.00 P A:PLP410 0.0 18.8 1.0 O3P A:PLP410 1.5 18.8 1.0 O1P A:PLP410 1.5 20.3 1.0 O2P A:PLP410 1.6 17.6 1.0 O4P A:PLP410 1.6 17.6 1.0 C5A A:PLP410 2.6 17.9 1.0 N A:GLY108 3.6 19.4 1.0 OG A:SER257 3.7 22.0 1.0 NH1 A:ARG266 3.7 15.0 1.0 NH2 A:ARG266 3.7 19.0 1.0 OH B:TYR70 3.9 17.7 1.0 OG A:SER255 3.9 18.5 1.0 C5 A:PLP410 4.0 20.5 1.0 N A:SER109 4.0 21.7 1.0 OG A:SER109 4.0 24.5 1.0 C4A A:PLP410 4.2 23.5 1.0 CZ A:ARG266 4.2 20.1 1.0 CA A:GLY107 4.3 14.0 1.0 CA A:GLY108 4.3 23.6 1.0 CB A:SER257 4.3 19.8 1.0 C A:GLY107 4.4 15.4 1.0 CB A:SER255 4.5 15.4 1.0 C4 A:PLP410 4.6 20.9 1.0 CB A:SER109 4.6 16.0 1.0 C A:GLY108 4.7 24.1 1.0 CE1 B:TYR70 4.8 13.6 1.0 CZ B:TYR70 4.8 16.8 1.0 CA A:SER109 4.9 14.6 1.0 C2' A:HCI411 4.9 35.6 1.0

Phosphorus binding site 2 out of 2 in the Aspartate Aminotransferase Hexamutant


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Aspartate Aminotransferase Hexamutant within 5.0Å range: probe atom residue distance (Å) B Occ B:P410 b:19.0 occ:1.00 P B:PLP410 0.0 19.0 1.0 O3P B:PLP410 1.5 19.9 1.0 O1P B:PLP410 1.5 19.4 1.0 O2P B:PLP410 1.5 14.0 1.0 O4P B:PLP410 1.6 20.2 1.0 C5A B:PLP410 2.6 20.9 1.0 N B:GLY108 3.7 17.8 1.0 OG B:SER257 3.7 21.8 1.0 OH A:TYR70 3.7 19.7 1.0 NH2 B:ARG266 3.8 23.9 1.0 NH1 B:ARG266 3.8 22.4 1.0 OG B:SER255 3.8 22.2 1.0 OG B:SER109 3.9 22.2 1.0 N B:SER109 4.0 15.6 1.0 C5 B:PLP410 4.0 25.3 1.0 C4A B:PLP410 4.2 30.5 1.0 CZ B:ARG266 4.3 23.4 1.0 CA B:GLY107 4.3 17.3 1.0 CB B:SER257 4.4 19.2 1.0 C B:GLY107 4.5 20.9 1.0 CA B:GLY108 4.5 19.2 1.0 CB B:SER109 4.5 15.2 1.0 CB B:SER255 4.5 20.2 1.0 CE1 A:TYR70 4.6 17.4 1.0 C4 B:PLP410 4.6 30.5 1.0 C B:GLY108 4.6 19.7 1.0 CZ A:TYR70 4.6 21.1 1.0 C2' B:HCI411 4.7 28.1 1.0 CA B:SER109 4.8 12.7 1.0 C3' B:HCI411 4.9 28.6 1.0

V.N.Malashkevich, J.J.Onuffer, J.F.Kirsch, J.N.Jansonius. Alternating Arginine-Modulated Substrate Specificity in An Engineered Tyrosine Aminotransferase. Nat.Struct.Biol. V. 2 548 1995.
ISSN: ISSN 1072-8368
PubMed: 7664122
DOI: 10.1038/NSB0795-548