Phosphorus in PDB 1acm: Arginine 54 in the Active Site of Escherichia Coli Aspartate Transcarbamoylase Is Critical For Catalysis: A Site-Specific Mutagenesis, uc(Nmr) and X-Ray Crystallography Study

Enzymatic activity of Arginine 54 in the Active Site of Escherichia Coli Aspartate Transcarbamoylase Is Critical For Catalysis: A Site-Specific Mutagenesis, uc(Nmr) and X-Ray Crystallography Study

All present enzymatic activity of Arginine 54 in the Active Site of Escherichia Coli Aspartate Transcarbamoylase Is Critical For Catalysis: A Site-Specific Mutagenesis, uc(Nmr) and X-Ray Crystallography Study:
2.1.3.2;

Protein crystallography data

The structure of Arginine 54 in the Active Site of Escherichia Coli Aspartate Transcarbamoylase Is Critical For Catalysis: A Site-Specific Mutagenesis, uc(Nmr) and X-Ray Crystallography Study, PDB code: 1acm was solved by R.C.Stevens, E.R.Kantrowitz, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.80
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 122.200, 122.200, 156.200, 90.00, 90.00, 120.00
R / Rfree (%) 18 / n/a

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the Arginine 54 in the Active Site of Escherichia Coli Aspartate Transcarbamoylase Is Critical For Catalysis: A Site-Specific Mutagenesis, uc(Nmr) and X-Ray Crystallography Study (pdb code 1acm). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the Arginine 54 in the Active Site of Escherichia Coli Aspartate Transcarbamoylase Is Critical For Catalysis: A Site-Specific Mutagenesis, uc(Nmr) and X-Ray Crystallography Study, PDB code: 1acm:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in 1acm

Go back to Phosphorus Binding Sites List in 1acm
Phosphorus binding site 1 out of 2 in the Arginine 54 in the Active Site of Escherichia Coli Aspartate Transcarbamoylase Is Critical For Catalysis: A Site-Specific Mutagenesis, uc(Nmr) and X-Ray Crystallography Study


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Arginine 54 in the Active Site of Escherichia Coli Aspartate Transcarbamoylase Is Critical For Catalysis: A Site-Specific Mutagenesis, uc(Nmr) and X-Ray Crystallography Study within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P311

b:12.3
occ:1.00
 P A:PAL311 0.0 12.3 1.0
O3P A:PAL311 1.6 16.5 1.0
O1P A:PAL311 1.6 9.0 1.0
O2P A:PAL311 1.6 9.9 1.0
C1P A:PAL311 1.8 8.6 1.0
C1 A:PAL311 2.8 19.8 1.0
O1 A:PAL311 3.3 26.6 1.0
N2 A:PAL311 3.6 19.4 1.0
NH1 A:ARG105 3.8 13.2 1.0
OG A:SER52 3.9 18.3 1.0
N A:ALA54 3.9 10.9 1.0
N A:THR53 3.9 5.2 1.0
O A:HOH315 4.0 12.2 1.0
OG1 A:THR55 4.0 9.1 1.0
N A:THR55 4.1 5.8 1.0
CA A:SER52 4.2 6.3 1.0
CB A:ALA54 4.2 9.9 1.0
NH2 A:ARG105 4.3 14.1 1.0
O3 A:PAL311 4.4 28.1 1.0
CA A:ALA54 4.4 9.8 1.0
CZ A:ARG105 4.5 9.3 1.0
CB A:SER52 4.6 7.8 1.0
C A:SER52 4.6 4.6 1.0
C A:THR53 4.7 11.3 1.0
CB A:THR55 4.7 6.8 1.0
C A:ALA54 4.7 9.6 1.0
O A:HOH313 4.8 13.0 1.0
C2 A:PAL311 4.8 17.0 1.0
O A:LEU267 4.9 13.6 1.0
CA A:THR53 4.9 6.8 1.0
O A:ALA51 4.9 4.9 1.0

Phosphorus binding site 2 out of 2 in 1acm

Go back to Phosphorus Binding Sites List in 1acm
Phosphorus binding site 2 out of 2 in the Arginine 54 in the Active Site of Escherichia Coli Aspartate Transcarbamoylase Is Critical For Catalysis: A Site-Specific Mutagenesis, uc(Nmr) and X-Ray Crystallography Study


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Arginine 54 in the Active Site of Escherichia Coli Aspartate Transcarbamoylase Is Critical For Catalysis: A Site-Specific Mutagenesis, uc(Nmr) and X-Ray Crystallography Study within 5.0Å range:
probe atom residue distance (Å) B Occ
C:P311

b:7.2
occ:1.00
 P C:PAL311 0.0 7.2 1.0
O1P C:PAL311 1.5 13.6 1.0
O2P C:PAL311 1.6 4.8 1.0
O3P C:PAL311 1.6 12.7 1.0
C1P C:PAL311 1.8 10.4 1.0
C1 C:PAL311 2.7 17.1 1.0
O1 C:PAL311 3.3 22.3 1.0
N2 C:PAL311 3.5 21.6 1.0
O C:HOH316 3.7 10.2 1.0
NH1 C:ARG105 3.8 12.0 1.0
N C:ALA54 3.8 4.9 1.0
N C:THR53 3.9 8.0 1.0
OG C:SER52 3.9 9.0 1.0
N C:THR55 3.9 5.8 1.0
OG1 C:THR55 4.1 2.0 1.0
CA C:SER52 4.2 4.5 1.0
CB C:ALA54 4.2 5.0 1.0
CA C:ALA54 4.4 3.4 1.0
CB C:SER52 4.4 7.8 1.0
CZ C:ARG105 4.6 9.2 1.0
NH2 C:ARG105 4.6 9.2 1.0
C C:SER52 4.6 8.4 1.0
C C:ALA54 4.6 4.8 1.0
CB C:THR55 4.6 6.6 1.0
C C:THR53 4.7 9.2 1.0
O C:LEU267 4.7 14.0 1.0
CA C:THR53 4.8 7.1 1.0
C2 C:PAL311 4.8 20.2 1.0
O C:HOH314 4.8 4.0 1.0
CD C:PRO268 4.8 2.0 1.0
O2 C:PAL311 4.9 22.1 1.0
CA C:THR55 4.9 8.0 1.0

Reference:

J.W.Stebbins, D.E.Robertson, M.F.Roberts, R.C.Stevens, W.N.Lipscomb, E.R.Kantrowitz. Arginine 54 in the Active Site of Escherichia Coli Aspartate Transcarbamoylase Is Critical For Catalysis: A Site-Specific Mutagenesis, uc(Nmr), and X-Ray Crystallographic Study. Protein Sci. V. 1 1435 1992.
ISSN: ISSN 0961-8368
PubMed: 1303763
Page generated: Fri Sep 25 12:45:00 2020

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