Phosphorus in PDB 1ahf: Aspartate Aminotransferase Hexamutant

All present enzymatic activity of Aspartate Aminotransferase Hexamutant:
2.6.1.1;

The structure of Aspartate Aminotransferase Hexamutant, PDB code: 1ahf 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 (°)	85.920, 79.390, 88.800, 90.00, 118.99, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Phosphorus atom in the Aspartate Aminotransferase Hexamutant (pdb code 1ahf). 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: 1ahf:
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:29.7 occ:1.00 P A:PLP410 0.0 29.7 1.0 O1P A:PLP410 1.5 19.9 1.0 O3P A:PLP410 1.5 27.6 1.0 O2P A:PLP410 1.6 32.3 1.0 O4P A:PLP410 1.6 26.1 1.0 C5A A:PLP410 2.5 32.1 1.0 N A:GLY108 3.5 24.9 1.0 OG A:SER257 3.6 21.7 1.0 NH1 A:ARG266 3.7 18.5 1.0 OH B:TYR70 3.7 29.4 1.0 OG A:SER255 3.7 21.5 1.0 NH2 A:ARG266 3.8 21.2 1.0 OG A:SER109 3.9 32.8 1.0 C5 A:PLP410 3.9 37.6 1.0 N A:SER109 3.9 28.7 1.0 C5 A:IOP411 4.0 58.8 1.0 C4A A:PLP410 4.2 51.6 1.0 CB A:SER257 4.2 17.4 1.0 CZ A:ARG266 4.2 21.7 1.0 CA A:GLY108 4.2 29.6 1.0 CA A:GLY107 4.3 26.4 1.0 C A:GLY107 4.3 24.8 1.0 CB A:SER255 4.5 18.6 1.0 CE1 B:TYR70 4.5 21.3 1.0 C4 A:PLP410 4.5 43.4 1.0 CB A:SER109 4.5 28.6 1.0 CZ B:TYR70 4.6 19.3 1.0 C A:GLY108 4.7 32.5 1.0 C4 A:IOP411 4.8 58.0 1.0 CA A:SER109 4.8 29.5 1.0 NZ A:LYS258 4.9 53.2 1.0 C6 A:IOP411 4.9 62.6 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:P412 b:30.1 occ:1.00 P B:PLP412 0.0 30.1 1.0 O3P B:PLP412 1.5 38.2 1.0 O1P B:PLP412 1.5 29.8 1.0 O4P B:PLP412 1.6 29.7 1.0 O2P B:PLP412 1.6 28.2 1.0 C5A B:PLP412 2.6 33.8 1.0 N B:GLY108 3.4 21.6 1.0 OG B:SER257 3.6 27.8 1.0 OG B:SER255 3.8 24.3 1.0 OH A:TYR70 3.8 22.7 1.0 NH2 B:ARG266 3.9 19.6 1.0 NH1 B:ARG266 3.9 25.6 1.0 C5 B:PLP412 4.0 36.2 1.0 N B:SER109 4.0 21.4 1.0 OG B:SER109 4.1 30.4 1.0 C4A B:PLP412 4.2 53.9 1.0 CB B:SER257 4.2 23.3 1.0 CA B:GLY108 4.2 23.3 1.0 CA B:GLY107 4.3 20.4 1.0 C B:GLY107 4.3 21.4 1.0 CZ B:ARG266 4.4 23.0 1.0 CB B:SER255 4.4 20.9 1.0 C4 B:PLP412 4.5 45.3 1.0 C B:GLY108 4.6 27.1 1.0 CE1 A:TYR70 4.6 16.8 1.0 CB B:SER109 4.6 26.8 1.0 CZ A:TYR70 4.7 15.0 1.0 NZ B:LYS258 4.8 55.6 1.0 CA B:SER109 4.9 26.3 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