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Zinc in PDB 4fyx: E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+

Enzymatic activity of E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+

All present enzymatic activity of E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+:
2.1.3.2;

Protein crystallography data

The structure of E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+, PDB code: 4fyx was solved by G.M.Cockrell, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.22 / 2.09
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 121.210, 121.210, 141.764, 90.00, 90.00, 120.00
R / Rfree (%) 16.5 / 21.3

Other elements in 4fyx:

The structure of E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+ also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+ (pdb code 4fyx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+, PDB code: 4fyx:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4fyx

Go back to Zinc Binding Sites List in 4fyx
Zinc binding site 1 out of 2 in the E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn201

b:24.0
occ:1.00
SG B:CYS114 2.3 24.2 1.0
SG B:CYS138 2.4 25.6 1.0
SG B:CYS141 2.4 24.2 1.0
SG B:CYS109 2.4 21.7 1.0
CB B:CYS138 3.0 30.3 1.0
CB B:CYS114 3.1 21.4 1.0
CB B:CYS109 3.2 23.0 1.0
CB B:CYS141 3.4 21.3 1.0
N B:CYS141 3.7 23.7 1.0
CA B:CYS141 4.1 26.5 1.0
CA B:CYS114 4.5 22.5 1.0
CA B:CYS138 4.5 30.4 1.0
OG B:SER116 4.5 23.3 1.0
CB B:ASN111 4.5 24.3 1.0
ND2 B:ASN111 4.6 24.4 1.0
CA B:CYS109 4.6 22.8 1.0
CB B:TYR140 4.7 23.3 1.0
C B:TYR140 4.8 23.7 1.0
O B:HOH392 4.9 22.9 1.0

Zinc binding site 2 out of 2 in 4fyx

Go back to Zinc Binding Sites List in 4fyx
Zinc binding site 2 out of 2 in the E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn201

b:22.9
occ:1.00
SG D:CYS109 2.3 21.4 1.0
SG D:CYS138 2.3 21.5 1.0
SG D:CYS114 2.4 23.5 1.0
SG D:CYS141 2.4 24.5 1.0
CB D:CYS138 3.1 20.0 1.0
CB D:CYS114 3.2 17.1 1.0
CB D:CYS109 3.2 21.3 1.0
CB D:CYS141 3.3 23.7 1.0
N D:CYS141 3.6 20.3 1.0
CA D:CYS141 4.1 22.5 1.0
OG D:SER116 4.4 21.0 1.0
CA D:CYS114 4.4 23.7 1.0
CB D:ASN111 4.5 27.4 1.0
CA D:CYS138 4.6 28.3 1.0
CA D:CYS109 4.6 19.5 1.0
CB D:TYR140 4.7 26.8 1.0
ND2 D:ASN111 4.7 23.8 1.0
C D:TYR140 4.8 24.2 1.0
O D:HOH309 4.8 24.6 1.0
C D:CYS141 5.0 22.6 1.0

Reference:

G.M.Cockrell, E.R.Kantrowitz. Metal Ion Involvement in the Allosteric Mechanism of Escherichia Coli Aspartate Transcarbamoylase. Biochemistry V. 51 7128 2012.
ISSN: ISSN 0006-2960
PubMed: 22906065
DOI: 10.1021/BI300920M
Page generated: Wed Dec 16 05:18:43 2020

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