Zinc in PDB 1tth: Aspartate Transcarbamoylase Catalytic Chain Mutant GLU50ALA Complexed with N-(Phosphonacetyl-L-Aspartate) (Pala)

All present enzymatic activity of Aspartate Transcarbamoylase Catalytic Chain Mutant GLU50ALA Complexed with N-(Phosphonacetyl-L-Aspartate) (Pala):
2.1.3.2;

The structure of Aspartate Transcarbamoylase Catalytic Chain Mutant GLU50ALA Complexed with N-(Phosphonacetyl-L-Aspartate) (Pala), PDB code: 1tth was solved by K.Stieglitz, B.Stec, D.P.Baker, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.80
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	122.240, 122.240, 156.360, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 26.4

The binding sites of Zinc atom in the Aspartate Transcarbamoylase Catalytic Chain Mutant GLU50ALA Complexed with N-(Phosphonacetyl-L-Aspartate) (Pala) (pdb code 1tth). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Aspartate Transcarbamoylase Catalytic Chain Mutant GLU50ALA Complexed with N-(Phosphonacetyl-L-Aspartate) (Pala), PDB code: 1tth:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Aspartate Transcarbamoylase Catalytic Chain Mutant GLU50ALA Complexed with N-(Phosphonacetyl-L-Aspartate) (Pala)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Aspartate Transcarbamoylase Catalytic Chain Mutant GLU50ALA Complexed with N-(Phosphonacetyl-L-Aspartate) (Pala) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn154 b:38.2 occ:1.00 SG B:CYS141 2.0 32.8 1.0 SG B:CYS109 2.1 28.0 1.0 SG B:CYS114 2.2 20.9 1.0 SG B:CYS138 2.4 22.2 1.0 CB B:CYS138 2.9 27.7 1.0 CB B:CYS114 3.1 23.9 1.0 CB B:CYS141 3.1 14.9 1.0 CB B:CYS109 3.3 34.7 1.0 N B:CYS141 3.7 12.0 1.0 CA B:CYS141 4.0 14.7 1.0 ND2 B:ASN111 4.1 54.4 1.0 CB B:ASN111 4.2 56.4 1.0 OG B:SER116 4.3 24.6 1.0 CA B:CYS114 4.4 21.0 1.0 CA B:CYS138 4.4 32.1 1.0 CB B:TYR140 4.6 9.2 1.0 CA B:CYS109 4.6 36.9 1.0 CG B:ASN111 4.7 49.3 1.0 O B:HOH166 4.7 16.4 1.0 C B:TYR140 4.9 15.0 1.0 C B:CYS141 4.9 19.6 1.0 C B:CYS138 5.0 27.9 1.0 CZ B:PHE145 5.0 38.0 1.0 N B:TYR140 5.0 18.2 1.0

Zinc binding site 2 out of 2 in the Aspartate Transcarbamoylase Catalytic Chain Mutant GLU50ALA Complexed with N-(Phosphonacetyl-L-Aspartate) (Pala)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Aspartate Transcarbamoylase Catalytic Chain Mutant GLU50ALA Complexed with N-(Phosphonacetyl-L-Aspartate) (Pala) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn155 b:30.5 occ:1.00 SG D:CYS141 2.2 33.2 1.0 SG D:CYS109 2.3 27.5 1.0 SG D:CYS114 2.3 30.4 1.0 SG D:CYS138 2.3 23.2 1.0 CB D:CYS138 2.8 19.9 1.0 CB D:CYS141 3.1 14.5 1.0 CB D:CYS109 3.2 16.4 1.0 CB D:CYS114 3.2 23.9 1.0 N D:CYS141 3.5 17.4 1.0 CA D:CYS141 3.9 18.8 1.0 CA D:CYS138 4.3 22.2 1.0 ND2 D:ASN111 4.4 41.2 1.0 CA D:CYS114 4.4 27.4 1.0 CB D:ASN111 4.5 45.2 1.0 CA D:CYS109 4.6 18.6 1.0 C D:TYR140 4.6 18.1 1.0 OG D:SER116 4.6 39.1 1.0 CB D:TYR140 4.7 12.3 1.0 C D:CYS141 4.8 24.1 1.0 C D:CYS138 4.8 20.9 1.0 N D:TYR140 4.8 22.1 1.0 N D:GLU142 4.9 21.0 1.0 CZ D:PHE145 4.9 33.7 1.0 CA D:TYR140 4.9 14.0 1.0 O D:CYS138 5.0 18.4 1.0 CG D:ASN111 5.0 42.2 1.0

K.Stieglitz, B.Stec, D.P.Baker, E.R.Kantrowitz. Monitoring the Transition From the T to the R State in E.Coli Aspartate Transcarbamoylase By X-Ray Crystallography: Crystal Structures of the E50A Mutant Enzyme in Four Distinct Allosteric States. J.Mol.Biol. V. 341 853 2004.
ISSN: ISSN 0022-2836
PubMed: 15288791
DOI: 10.1016/J.JMB.2004.06.002