Phosphorus in PDB 1ahg: Aspartate Aminotransferase Hexamutant

All present enzymatic activity of Aspartate Aminotransferase Hexamutant:
2.6.1.1;

The structure of Aspartate Aminotransferase Hexamutant, PDB code: 1ahg 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 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	86.000, 79.100, 89.600, 90.00, 118.67, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Phosphorus atom in the Aspartate Aminotransferase Hexamutant (pdb code 1ahg). 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: 1ahg:
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:P500 b:25.0 occ:1.00 P A:PLP500 0.0 25.0 1.0 O3P A:PLP500 1.4 20.9 1.0 O2P A:PLP500 1.5 27.2 1.0 O1P A:PLP500 1.6 24.0 1.0 O4P A:PLP500 1.6 22.9 1.0 C5A A:PLP500 2.6 19.7 1.0 OH B:TYR70 3.6 8.3 1.0 N A:GLY108 3.6 22.2 1.0 NH1 A:ARG266 3.8 9.0 1.0 OG A:SER257 4.0 21.8 1.0 NH2 A:ARG266 4.0 11.6 1.0 C5 A:PLP500 4.0 20.4 1.0 OG A:SER109 4.0 11.1 1.0 OG A:SER255 4.0 6.2 1.0 N A:SER109 4.1 12.9 1.0 CA A:GLY108 4.2 22.1 1.0 C4A A:PLP500 4.3 18.4 1.0 CB A:SER255 4.3 9.4 1.0 CZ A:ARG266 4.4 13.0 1.0 CB A:SER257 4.4 20.4 1.0 CA A:GLY107 4.5 9.7 1.0 C A:GLY107 4.6 19.7 1.0 NZ A:LYS258 4.6 22.2 1.0 C4 A:PLP500 4.6 17.8 1.0 CZ B:TYR70 4.6 5.5 1.0 C A:GLY108 4.7 19.7 1.0 CE1 B:TYR70 4.7 4.4 1.0 CB A:SER109 4.9 10.6 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:P500 b:16.7 occ:1.00 P B:PLP500 0.0 16.7 1.0 O3P B:PLP500 1.5 18.0 1.0 O1P B:PLP500 1.5 8.1 1.0 O4P B:PLP500 1.6 19.0 1.0 O2P B:PLP500 1.6 15.9 1.0 C5A B:PLP500 2.6 20.4 1.0 N B:GLY108 3.5 18.1 1.0 NH2 B:ARG266 3.5 24.4 1.0 OH A:TYR70 3.6 14.1 1.0 NH1 B:ARG266 3.8 33.5 1.0 C5 B:PLP500 3.8 22.9 1.0 OG B:SER255 3.8 21.6 1.0 OG B:SER109 3.9 20.9 1.0 N B:SER109 3.9 17.3 1.0 CZ B:ARG266 4.1 27.6 1.0 OG B:SER257 4.2 29.4 1.0 CA B:GLY108 4.3 16.8 1.0 CA B:GLY107 4.4 19.9 1.0 C B:GLY107 4.4 22.1 1.0 C4A B:PLP500 4.5 25.1 1.0 CB B:SER109 4.5 14.2 1.0 C B:GLY108 4.5 21.3 1.0 C6 B:PLP500 4.5 20.7 1.0 C4 B:PLP500 4.6 23.2 1.0 CZ A:TYR70 4.6 8.3 1.0 CE1 A:TYR70 4.7 10.9 1.0 CB B:SER257 4.7 24.1 1.0 CA B:SER109 4.8 14.6 1.0 CB B:SER255 4.8 17.9 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