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Zinc 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

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc 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 Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1acm

Go back to Zinc Binding Sites List in 1acm
Zinc 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 Zinc with other atoms in the Zn 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
B:Zn154

b:18.9
occ:1.00
SG B:CYS114 2.3 20.9 1.0
SG B:CYS141 2.3 13.8 1.0
SG B:CYS138 2.3 14.5 1.0
SG B:CYS109 2.3 21.7 1.0
CB B:CYS138 3.1 17.6 1.0
CB B:CYS109 3.2 21.7 1.0
CB B:CYS141 3.2 17.4 1.0
CB B:CYS114 3.2 17.1 1.0
N B:CYS141 3.6 12.7 1.0
CA B:CYS141 4.0 15.0 1.0
CB B:ASN111 4.2 14.8 1.0
OG B:SER116 4.3 24.7 1.0
CA B:CYS114 4.4 11.6 1.0
CA B:CYS138 4.5 18.2 1.0
CA B:CYS109 4.6 23.4 1.0
C B:TYR140 4.8 9.4 1.0
C B:CYS141 4.8 15.0 1.0
ND2 B:ASN111 4.8 23.1 1.0
CE2 B:PHE145 4.9 35.3 1.0
CB B:TYR140 4.9 8.1 1.0
CG B:ASN111 5.0 15.1 1.0
N B:GLU142 5.0 20.0 1.0

Zinc binding site 2 out of 2 in 1acm

Go back to Zinc Binding Sites List in 1acm
Zinc 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 Zinc with other atoms in the Zn 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
D:Zn154

b:18.7
occ:1.00
SG D:CYS138 2.3 17.1 1.0
SG D:CYS109 2.4 18.4 1.0
SG D:CYS114 2.4 17.0 1.0
SG D:CYS141 2.4 16.1 1.0
CB D:CYS138 3.1 19.0 1.0
CB D:CYS114 3.2 16.5 1.0
CB D:CYS109 3.3 15.1 1.0
CB D:CYS141 3.4 12.1 1.0
N D:CYS141 3.7 10.9 1.0
CA D:CYS141 4.1 10.6 1.0
CA D:CYS114 4.5 14.0 1.0
CA D:CYS138 4.5 11.4 1.0
CB D:ASN111 4.6 18.3 1.0
CA D:CYS109 4.6 16.5 1.0
ND2 D:ASN111 4.6 14.0 1.0
C D:TYR140 4.8 8.6 1.0
OG D:SER116 4.8 22.9 1.0
CB D:TYR140 4.9 7.4 1.0
C D:CYS141 5.0 10.0 1.0
CB D:SER116 5.0 12.5 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: Wed Dec 16 02:44:31 2020

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