Zinc in PDB 3mpu: Crystal Structure of the C47A/A241C Disulfide-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme

All present enzymatic activity of Crystal Structure of the C47A/A241C Disulfide-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme:
2.1.3.2;

The structure of Crystal Structure of the C47A/A241C Disulfide-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme, PDB code: 3mpu was solved by K.R.Mendes, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.92 / 2.85
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	120.711, 120.711, 692.471, 90.00, 90.00, 120.00
R / Rfree (%)	17.3 / 24

The binding sites of Zinc atom in the Crystal Structure of the C47A/A241C Disulfide-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme (pdb code 3mpu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the C47A/A241C Disulfide-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme, PDB code: 3mpu:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of the C47A/A241C Disulfide-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme


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 the C47A/A241C Disulfide-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn154 b:59.4 occ:1.00 SG B:CYS109 2.3 56.0 1.0 SG B:CYS138 2.4 54.1 1.0 SG B:CYS114 2.4 52.9 1.0 SG B:CYS141 2.6 54.3 1.0 CB B:CYS114 3.0 49.4 1.0 CB B:CYS109 3.2 54.9 1.0 CB B:CYS138 3.2 54.5 1.0 CB B:CYS141 3.4 53.0 1.0 N B:CYS141 3.6 50.1 1.0 CA B:CYS141 4.1 52.0 1.0 O B:HOH304 4.2 70.6 1.0 CA B:CYS114 4.3 50.3 1.0 OG B:SER116 4.5 55.5 1.0 CB B:ASN111 4.5 58.1 1.0 CA B:CYS109 4.6 56.7 1.0 CB B:TYR140 4.6 51.5 1.0 CA B:CYS138 4.7 54.7 1.0 ND2 B:ASN111 4.7 49.4 1.0 C B:TYR140 4.8 49.7 1.0 C B:CYS141 5.0 55.4 1.0 O B:HOH327 5.0 57.9 1.0 N B:TYR140 5.0 49.5 1.0 CA B:TYR140 5.0 53.5 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of the C47A/A241C Disulfide-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme


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 the C47A/A241C Disulfide-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn154 b:55.2 occ:1.00 SG D:CYS141 2.3 55.9 1.0 SG D:CYS109 2.3 65.9 1.0 SG D:CYS114 2.4 47.4 1.0 SG D:CYS138 2.4 52.3 1.0 CB D:CYS138 3.0 50.3 1.0 CB D:CYS109 3.1 54.2 1.0 CB D:CYS141 3.3 53.2 1.0 CB D:CYS114 3.4 53.5 1.0 N D:CYS141 3.7 48.9 1.0 CA D:CYS141 4.1 49.0 1.0 OG D:SER116 4.4 56.4 1.0 O D:HOH200 4.5 59.0 1.0 CA D:CYS138 4.5 48.5 1.0 CB D:ASN111 4.5 55.2 1.0 CA D:CYS109 4.6 61.8 1.0 CA D:CYS114 4.6 49.8 1.0 CB D:TYR140 4.7 52.5 1.0 O D:HOH316 4.8 56.2 1.0 C D:TYR140 4.9 51.1 1.0 ND2 D:ASN111 4.9 61.2 1.0 C D:CYS141 5.0 51.0 1.0 N D:GLU142 5.0 49.9 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of the C47A/A241C Disulfide-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the C47A/A241C Disulfide-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn154 b:58.1 occ:1.00 SG F:CYS138 2.3 53.1 1.0 SG F:CYS109 2.3 63.1 1.0 SG F:CYS114 2.4 52.8 1.0 SG F:CYS141 2.5 56.0 1.0 CB F:CYS138 3.0 59.3 1.0 CB F:CYS109 3.2 64.2 1.0 CB F:CYS114 3.3 58.1 1.0 CB F:CYS141 3.3 54.2 1.0 N F:CYS141 3.6 59.7 1.0 CA F:CYS141 4.0 50.8 1.0 CA F:CYS138 4.5 58.0 1.0 OG F:SER116 4.6 61.2 1.0 CA F:CYS114 4.6 55.6 1.0 CB F:TYR140 4.7 52.2 1.0 CA F:CYS109 4.7 64.0 1.0 C F:TYR140 4.8 54.3 1.0 C F:CYS141 4.9 55.6 1.0 CB F:ASN111 4.9 62.1 1.0 CB F:SER116 5.0 58.4 1.0 N F:GLU142 5.0 55.6 1.0 N F:TYR140 5.0 52.5 1.0

K.R.Mendes, E.R.Kantrowitz. The Pathway of Product Release From the R State of Aspartate Transcarbamoylase. J.Mol.Biol. V. 401 940 2010.
ISSN: ISSN 0022-2836
PubMed: 20620149
DOI: 10.1016/J.JMB.2010.07.003