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Zinc in PDB 3d7s: Crystal Structure of Wild-Type E. Coli Asparate Transcarbamoylase at pH 8.5 at 2.80 A Resolution

Enzymatic activity of Crystal Structure of Wild-Type E. Coli Asparate Transcarbamoylase at pH 8.5 at 2.80 A Resolution

All present enzymatic activity of Crystal Structure of Wild-Type E. Coli Asparate Transcarbamoylase at pH 8.5 at 2.80 A Resolution:
2.1.3.2;

Protein crystallography data

The structure of Crystal Structure of Wild-Type E. Coli Asparate Transcarbamoylase at pH 8.5 at 2.80 A Resolution, PDB code: 3d7s was solved by K.A.Stieglitz, J.Xia, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.80
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 129.680, 129.680, 198.580, 90.00, 90.00, 120.00
R / Rfree (%) 20.6 / 23.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Wild-Type E. Coli Asparate Transcarbamoylase at pH 8.5 at 2.80 A Resolution (pdb code 3d7s). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Wild-Type E. Coli Asparate Transcarbamoylase at pH 8.5 at 2.80 A Resolution, PDB code: 3d7s:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3d7s

Go back to Zinc Binding Sites List in 3d7s
Zinc binding site 1 out of 2 in the Crystal Structure of Wild-Type E. Coli Asparate Transcarbamoylase at pH 8.5 at 2.80 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Wild-Type E. Coli Asparate Transcarbamoylase at pH 8.5 at 2.80 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn313

b:91.8
occ:1.00
SG B:CYS138 1.9 54.7 1.0
CB B:CYS138 2.4 60.4 1.0
N B:CYS141 2.5 53.5 1.0
SG B:CYS114 2.6 52.5 1.0
SG B:CYS141 2.7 51.4 1.0
C B:CYS138 2.7 61.4 1.0
CA B:CYS138 2.9 62.3 1.0
O B:CYS138 2.9 65.8 1.0
N B:TYR140 3.0 53.2 1.0
CB B:CYS141 3.2 51.4 1.0
CA B:CYS141 3.3 51.1 1.0
C B:TYR140 3.3 53.0 1.0
N B:LYS139 3.4 57.5 1.0
CA B:TYR140 3.4 51.4 1.0
CB B:TYR140 3.5 49.9 1.0
SG B:CYS109 3.7 52.8 1.0
O B:HOH314 3.7 35.3 1.0
N B:GLU142 3.8 52.5 1.0
C B:LYS139 3.9 53.8 1.0
C B:CYS141 4.0 53.1 1.0
CA B:LYS139 4.2 52.4 1.0
CB B:CYS109 4.3 50.2 1.0
N B:CYS138 4.3 62.4 1.0
O B:TYR140 4.4 55.1 1.0
CG B:TYR140 4.5 48.9 1.0
CB B:CYS114 4.5 54.8 1.0
CD2 B:TYR140 4.5 49.3 1.0
OG B:SER116 4.7 55.3 1.0
O B:LYS139 4.9 53.5 1.0
O B:SER124 4.9 53.5 1.0
CA B:GLU142 5.0 53.4 1.0

Zinc binding site 2 out of 2 in 3d7s

Go back to Zinc Binding Sites List in 3d7s
Zinc binding site 2 out of 2 in the Crystal Structure of Wild-Type E. Coli Asparate Transcarbamoylase at pH 8.5 at 2.80 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Wild-Type E. Coli Asparate Transcarbamoylase at pH 8.5 at 2.80 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn314

b:99.7
occ:1.00
SG D:CYS138 1.9 56.5 1.0
CB D:CYS109 2.0 55.8 1.0
SG D:CYS114 2.0 57.0 1.0
SG D:CYS109 2.3 56.5 1.0
CB D:CYS114 3.0 60.4 1.0
O D:CYS114 3.2 60.4 1.0
SG D:CYS141 3.4 57.1 1.0
O D:HOH335 3.4 48.5 1.0
CA D:CYS109 3.6 57.1 1.0
OG D:SER116 3.6 58.4 1.0
CB D:CYS138 3.7 59.5 1.0
C D:CYS114 4.0 59.8 1.0
CA D:CYS114 4.1 59.9 1.0
N D:CYS109 4.1 59.5 1.0
CB D:CYS141 4.2 51.4 1.0
N D:CYS141 4.3 46.5 1.0
CB D:TYR140 4.4 52.1 1.0
C D:CYS109 4.5 57.0 1.0
O D:CYS109 4.5 57.5 1.0
CA D:CYS138 4.6 59.3 1.0
CB D:SER116 4.8 61.9 1.0
N D:TYR140 4.9 51.1 1.0
CZ D:PHE125 4.9 63.3 1.0
CA D:CYS141 4.9 47.8 1.0
CE2 D:PHE125 5.0 62.8 1.0
O D:HOH345 5.0 0.7 1.0

Reference:

K.A.Stieglitz, J.Xia, E.R.Kantrowitz. The First High pH Structure of Escherichia Coli Aspartate Transcarbamoylase. Proteins V. 74 318 2008.
ISSN: ISSN 0887-3585
PubMed: 18618694
DOI: 10.1002/PROT.22162
Page generated: Wed Dec 16 04:12:22 2020

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