Zinc in PDB 1sku: E. Coli Aspartate Transcarbamylase 240'S Loop Mutant (K244N)

All present enzymatic activity of E. Coli Aspartate Transcarbamylase 240'S Loop Mutant (K244N):
2.1.3.2;

The structure of E. Coli Aspartate Transcarbamylase 240'S Loop Mutant (K244N), PDB code: 1sku was solved by N.Alam, K.A.Stieglitz, M.D.Caban, S.Gourinath, H.Tsuruta, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.55 / 2.60
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	125.670, 125.670, 198.200, 90.00, 90.00, 120.00
R / Rfree (%)	20.1 / 23.1

The binding sites of Zinc atom in the E. Coli Aspartate Transcarbamylase 240'S Loop Mutant (K244N) (pdb code 1sku). 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 Transcarbamylase 240'S Loop Mutant (K244N), PDB code: 1sku:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the E. Coli Aspartate Transcarbamylase 240'S Loop Mutant (K244N)


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 Transcarbamylase 240'S Loop Mutant (K244N) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn315 b:84.9 occ:1.00 SG B:CYS114 2.3 19.4 1.0 SG B:CYS138 2.5 15.6 1.0 SG B:CYS109 2.9 21.2 1.0 CB B:CYS109 3.1 5.7 1.0 OG B:SER116 3.4 22.0 1.0 CB B:CYS141 3.5 3.8 1.0 CB B:CYS114 3.7 21.8 1.0 CB B:CYS138 3.8 27.3 1.0 N B:CYS141 3.8 11.6 1.0 CB B:SER116 4.2 23.0 1.0 CB B:TYR140 4.2 18.0 1.0 CA B:CYS141 4.3 10.6 1.0 CA B:CYS109 4.6 11.4 1.0 SG B:CYS141 4.6 42.1 1.0 C B:TYR140 4.8 14.6 1.0 CA B:TYR140 5.0 18.7 1.0 CG B:TYR140 5.0 19.6 1.0 N B:TYR140 5.0 20.1 1.0

Zinc binding site 2 out of 2 in the E. Coli Aspartate Transcarbamylase 240'S Loop Mutant (K244N)


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 Transcarbamylase 240'S Loop Mutant (K244N) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn314 b:59.8 occ:1.00 SG D:CYS114 2.2 11.8 1.0 SG D:CYS138 2.2 6.1 1.0 SG D:CYS141 2.3 4.3 1.0 SG D:CYS109 2.4 2.2 1.0 CB D:CYS109 3.2 3.1 1.0 CB D:CYS114 3.2 22.8 1.0 CB D:CYS138 3.3 24.9 1.0 CB D:CYS141 3.6 10.4 1.0 N D:CYS141 3.9 15.2 1.0 OG D:SER116 4.2 16.0 1.0 CA D:CYS141 4.4 13.3 1.0 CA D:CYS114 4.5 26.2 1.0 CB D:ASN111 4.6 11.0 1.0 CA D:CYS109 4.7 6.5 1.0 CA D:CYS138 4.7 24.6 1.0 CB D:TYR140 4.8 0.0 1.0 O D:ASN111 4.9 22.2 1.0

N.Alam, K.A.Stieglitz, M.D.Caban, S.Gourinath, H.Tsuruta, E.R.Kantrowitz. 240S Loop Interactions Stabilize the T State of Escherichia Coli Aspartate Transcarbamoylase. J.Biol.Chem. V. 279 23302 2004.
ISSN: ISSN 0021-9258
PubMed: 15014067
DOI: 10.1074/JBC.M401637200