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

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy