Phosphorus in PDB 1ahe: Aspartate Aminotransferase Hexamutant

All present enzymatic activity of Aspartate Aminotransferase Hexamutant:
2.6.1.1;

The structure of Aspartate Aminotransferase Hexamutant, PDB code: 1ahe 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 (°)	85.070, 77.980, 88.860, 90.00, 118.63, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Phosphorus atom in the Aspartate Aminotransferase Hexamutant (pdb code 1ahe). 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: 1ahe:
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:P412 b:25.5 occ:1.00 P A:PLP412 0.0 25.5 1.0 O3P A:PLP412 1.4 26.1 1.0 O1P A:PLP412 1.5 27.0 1.0 O4P A:PLP412 1.5 27.6 1.0 O2P A:PLP412 1.6 27.2 1.0 C5A A:PLP412 2.6 32.3 1.0 N A:GLY108 3.4 22.5 1.0 OG A:SER257 3.4 27.9 1.0 OG A:SER255 3.7 23.2 1.0 NH2 A:ARG266 3.8 17.9 1.0 NH1 A:ARG266 3.9 22.6 1.0 OH B:TYR70 3.9 30.6 1.0 C5 A:PLP412 3.9 33.8 1.0 N A:SER109 4.0 25.9 1.0 O B:HOH437 4.1 46.5 1.0 C4A A:PLP412 4.1 40.9 1.0 CA A:GLY107 4.1 22.7 1.0 C A:GLY107 4.2 23.3 1.0 CA A:GLY108 4.2 24.3 1.0 CZ A:ARG266 4.3 21.8 1.0 CB A:SER255 4.3 20.6 1.0 OG A:SER109 4.3 35.4 1.0 CB A:SER257 4.3 24.1 1.0 CB A:SER109 4.4 30.1 1.0 C4 A:PLP412 4.4 36.6 1.0 C A:GLY108 4.7 29.6 1.0 CE1 B:TYR70 4.7 24.8 1.0 CZ B:TYR70 4.8 26.7 1.0 CA A:SER109 4.8 25.6 1.0 NZ A:LYS258 4.9 42.8 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:P412 b:28.3 occ:1.00 P B:PLP412 0.0 28.3 1.0 O1P B:PLP412 1.5 33.3 1.0 O3P B:PLP412 1.5 26.6 1.0 O2P B:PLP412 1.5 28.9 1.0 O4P B:PLP412 1.5 30.4 1.0 C5A B:PLP412 2.6 36.0 1.0 N B:GLY108 3.4 24.1 1.0 OG B:SER257 3.4 28.9 1.0 OG B:SER255 3.8 25.8 1.0 OH A:TYR70 3.8 26.8 1.0 NH2 B:ARG266 3.8 17.2 1.0 NH1 B:ARG266 4.0 21.7 1.0 O B:HOH414 4.0 70.6 1.0 C5 B:PLP412 4.0 39.3 1.0 N B:SER109 4.0 22.2 1.0 OG B:SER109 4.1 32.5 1.0 C4A B:PLP412 4.1 49.1 1.0 CA B:GLY107 4.2 29.4 1.0 CB B:SER257 4.2 27.2 1.0 CA B:GLY108 4.2 22.5 1.0 C B:GLY107 4.3 28.6 1.0 CB B:SER255 4.3 22.0 1.0 CZ B:ARG266 4.4 21.6 1.0 C4 B:PLP412 4.5 45.8 1.0 CB B:SER109 4.6 27.8 1.0 CE1 A:TYR70 4.6 21.3 1.0 C B:GLY108 4.6 26.7 1.0 CZ A:TYR70 4.7 21.8 1.0 CA B:SER109 4.9 24.1 1.0 NZ B:LYS258 5.0 50.6 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