Phosphorus in PDB 1ahy: Aspartate Aminotransferase Hexamutant

All present enzymatic activity of Aspartate Aminotransferase Hexamutant:
2.6.1.1;

The structure of Aspartate Aminotransferase Hexamutant, PDB code: 1ahy 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 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	85.930, 79.090, 89.720, 90.00, 118.70, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Phosphorus atom in the Aspartate Aminotransferase Hexamutant (pdb code 1ahy). 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: 1ahy:
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:27.7 occ:1.00 P A:PLP410 0.0 27.7 1.0 O3P A:PLP410 1.5 22.0 1.0 O1P A:PLP410 1.5 34.1 1.0 O2P A:PLP410 1.5 25.3 1.0 O4P A:PLP410 1.6 28.9 1.0 C5A A:PLP410 2.6 27.7 1.0 N A:GLY108 3.6 23.5 1.0 NH1 A:ARG266 3.7 21.1 1.0 OG A:SER255 3.7 23.9 1.0 NH2 A:ARG266 3.8 25.5 1.0 OG A:SER257 3.9 28.3 1.0 OH B:TYR70 3.9 20.2 1.0 C5 A:PLP410 3.9 24.7 1.0 N A:SER109 4.0 28.4 1.0 O A:HOH435 4.0 45.6 1.0 OG A:SER109 4.1 27.0 1.0 C4A A:PLP410 4.1 30.7 1.0 CA A:GLY108 4.2 26.9 1.0 CZ A:ARG266 4.2 22.4 1.0 CB A:SER257 4.3 27.8 1.0 CA A:GLY107 4.4 24.1 1.0 C A:GLY107 4.4 26.6 1.0 C4 A:PLP410 4.5 26.3 1.0 CB A:SER255 4.5 25.9 1.0 C A:GLY108 4.6 29.3 1.0 CB A:SER109 4.6 25.8 1.0 CE1 B:TYR70 4.7 15.9 1.0 CZ B:TYR70 4.8 17.2 1.0 CA A:SER109 4.9 28.0 1.0 C6 A:PLP410 5.0 24.6 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:30.1 occ:1.00 P B:PLP410 0.0 30.1 1.0 O3P B:PLP410 1.5 26.2 1.0 O1P B:PLP410 1.5 34.6 1.0 O2P B:PLP410 1.6 32.3 1.0 O4P B:PLP410 1.6 25.5 1.0 C5A B:PLP410 2.6 25.1 1.0 NH2 B:ARG266 3.5 28.3 1.0 N B:GLY108 3.7 23.0 1.0 OG B:SER255 3.8 27.9 1.0 NH1 B:ARG266 3.8 23.7 1.0 O B:HOH439 3.9 32.1 1.0 C5 B:PLP410 3.9 28.1 1.0 OG B:SER257 4.0 28.8 1.0 OH A:TYR70 4.0 28.3 1.0 OG B:SER109 4.0 32.9 1.0 N B:SER109 4.1 25.9 1.0 CZ B:ARG266 4.1 24.2 1.0 C4A B:PLP410 4.2 40.2 1.0 CB B:SER257 4.3 27.7 1.0 CA B:GLY108 4.4 26.0 1.0 CA B:GLY107 4.4 20.8 1.0 C B:GLY107 4.5 26.6 1.0 C4 B:PLP410 4.5 36.1 1.0 C B:GLY108 4.6 30.1 1.0 CB B:SER109 4.6 26.4 1.0 CB B:SER255 4.7 30.9 1.0 CE1 A:TYR70 4.7 24.5 1.0 CZ A:TYR70 4.8 25.6 1.0 CA B:SER109 4.9 26.5 1.0 NZ B:LYS258 5.0 39.5 1.0 C6 B:PLP410 5.0 25.9 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