Phosphorus in PDB 12as: Asparagine Synthetase Mutant C51A, C315A Complexed with L- Asparagine and Amp

All present enzymatic activity of Asparagine Synthetase Mutant C51A, C315A Complexed with L- Asparagine and Amp:
6.3.1.1;

The structure of Asparagine Synthetase Mutant C51A, C315A Complexed with L- Asparagine and Amp, PDB code: 12as was solved by T.Nakatsu, H.Kato, J.Oda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	53.000, 126.130, 52.860, 90.00, 105.59, 90.00
R / Rfree (%)	16.4 / 28.7

The binding sites of Phosphorus atom in the Asparagine Synthetase Mutant C51A, C315A Complexed with L- Asparagine and Amp (pdb code 12as). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the Asparagine Synthetase Mutant C51A, C315A Complexed with L- Asparagine and Amp, PDB code: 12as:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in the Asparagine Synthetase Mutant C51A, C315A Complexed with L- Asparagine and Amp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Asparagine Synthetase Mutant C51A, C315A Complexed with L- Asparagine and Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:P332 b:27.6 occ:1.00 P A:AMP332 0.0 27.6 1.0 O2P A:AMP332 1.5 32.6 1.0 O1P A:AMP332 1.5 54.2 1.0 O3P A:AMP332 1.6 28.3 1.0 O5' A:AMP332 1.7 10.4 1.0 C5' A:AMP332 2.7 13.4 1.0 ND2 A:ASN331 3.7 21.2 1.0 CG A:ASN331 3.8 12.3 1.0 NH1 A:ARG100 3.8 21.8 1.0 C4' A:AMP332 4.0 9.3 1.0 OD1 A:ASN331 4.0 35.1 1.0 C8 A:AMP332 4.2 13.2 1.0 OG A:SER251 4.2 14.9 1.0 O4' A:AMP332 4.4 23.9 1.0 C3' A:AMP332 4.4 29.4 1.0 NH2 A:ARG100 4.4 9.6 1.0 CB A:ASN331 4.5 25.2 1.0 OE1 A:GLN116 4.6 2.0 1.0 CZ A:ARG100 4.6 16.4 1.0 CB A:SER251 4.9 2.4 1.0

Phosphorus binding site 2 out of 2 in the Asparagine Synthetase Mutant C51A, C315A Complexed with L- Asparagine and Amp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Asparagine Synthetase Mutant C51A, C315A Complexed with L- Asparagine and Amp within 5.0Å range: probe atom residue distance (Å) B Occ B:P332 b:25.5 occ:1.00 P B:AMP332 0.0 25.5 1.0 O2P B:AMP332 1.5 13.9 1.0 O1P B:AMP332 1.5 30.0 1.0 O3P B:AMP332 1.6 27.1 1.0 O5' B:AMP332 1.6 12.3 1.0 C5' B:AMP332 2.7 8.3 1.0 NH1 B:ARG100 3.7 2.0 1.0 OG B:SER251 3.8 2.9 1.0 O B:HOH385 3.9 3.4 1.0 C4' B:AMP332 3.9 10.8 1.0 C3' B:AMP332 4.2 5.2 1.0 C8 B:AMP332 4.2 9.4 1.0 ND2 B:ASN331 4.2 19.2 1.0 NH2 B:ARG100 4.4 2.0 1.0 O4' B:AMP332 4.5 2.6 1.0 CB B:SER251 4.5 2.8 1.0 CZ B:ARG100 4.5 2.0 1.0 CB B:ASN331 4.6 23.7 1.0 CG B:ASN331 4.6 24.1 1.0 O3' B:AMP332 4.9 3.0 1.0 OE1 B:GLN116 4.9 2.2 1.0

T.Nakatsu, H.Kato, J.Oda. Crystal Structure of Asparagine Synthetase Reveals A Close Evolutionary Relationship to Class II Aminoacyl-Trna Synthetase. Nat.Struct.Biol. V. 5 15 1998.
ISSN: ISSN 1072-8368
PubMed: 9437423
DOI: 10.1038/NSB0198-15