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

Enzymatic activity of 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;

Protein crystallography data

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

Phosphorus Binding Sites:

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 12as

Go back to Phosphorus Binding Sites List in 12as
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 12as

Go back to Phosphorus Binding Sites List in 12as
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

Reference:

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
Page generated: Fri Sep 25 11:18:15 2020

Last articles

Zn in 7M6U
Zn in 7NNG
Zn in 7NEE
Zn in 7NEU
Zn in 7M3K
Zn in 7KWD
Zn in 7KYH
Zn in 7KNG
Zn in 7KY2
Zn in 7KYF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy