Zinc in PDB 7z19: E. Coli C-P Lyase Bound to A Single Phnk Abc Domain

All present enzymatic activity of E. Coli C-P Lyase Bound to A Single Phnk Abc Domain:
2.7.8.37; 4.7.1.1;

The binding sites of Zinc atom in the E. Coli C-P Lyase Bound to A Single Phnk Abc Domain (pdb code 7z19). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the E. Coli C-P Lyase Bound to A Single Phnk Abc Domain, PDB code: 7z19:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the E. Coli C-P Lyase Bound to A Single Phnk Abc Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of E. Coli C-P Lyase Bound to A Single Phnk Abc Domain within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn401 b:80.7 occ:0.51 NE2 C:HIS328 2.1 70.3 1.0 NE2 C:HIS333 2.1 70.6 1.0 HE2 D:HIS108 3.0 70.6 1.0 CE1 C:HIS328 3.0 70.3 1.0 CE1 C:HIS333 3.1 70.6 1.0 CD2 C:HIS328 3.1 70.3 1.0 CD2 C:HIS333 3.1 70.6 1.0 HE1 D:HIS108 3.2 70.6 1.0 HH21 D:ARG107 3.2 70.3 1.0 HE1 C:HIS328 3.2 70.3 1.0 HE1 C:HIS333 3.2 70.6 1.0 HG3 D:PRO126 3.3 72.2 1.0 HD2 C:HIS328 3.3 70.3 1.0 HD2 C:HIS333 3.3 70.6 1.0 NE2 D:HIS108 3.5 70.6 1.0 CE1 D:HIS108 3.7 70.6 1.0 NH2 D:ARG107 3.9 70.3 1.0 HG2 D:PRO187 4.1 70.5 1.0 HH22 D:ARG107 4.1 70.3 1.0 ND1 C:HIS328 4.1 70.3 1.0 HB3 D:PRO126 4.1 72.2 1.0 CG C:HIS328 4.2 70.3 1.0 CG D:PRO126 4.2 72.2 1.0 ND1 C:HIS333 4.2 70.6 1.0 CG C:HIS333 4.2 70.6 1.0 HE D:ARG107 4.5 70.3 1.0 HG2 D:PRO126 4.6 72.2 1.0 HE1 C:PHE325 4.6 71.3 1.0 CB D:PRO126 4.6 72.2 1.0 CZ D:ARG107 4.8 70.3 1.0 CD2 D:HIS108 4.9 70.6 1.0 HB2 D:PRO126 4.9 72.2 1.0 HD3 D:PRO126 4.9 72.2 1.0 HD21 C:LEU329 4.9 71.2 1.0 HD1 C:HIS328 4.9 70.3 1.0 ND1 D:HIS108 5.0 70.6 1.0 HD1 C:HIS333 5.0 70.6 1.0

Zinc binding site 2 out of 4 in the E. Coli C-P Lyase Bound to A Single Phnk Abc Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of E. Coli C-P Lyase Bound to A Single Phnk Abc Domain within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn301 b:110.6 occ:1.00 SG D:CYS266 2.2 79.7 1.0 SG D:CYS272 2.2 81.8 1.0 SG D:CYS241 2.3 80.2 1.0 SG D:CYS244 2.3 82.4 1.0 HB2 D:CYS266 2.4 79.7 1.0 CB D:CYS266 2.8 79.7 1.0 H D:CYS266 2.9 79.7 1.0 HB2 D:CYS241 3.1 80.2 1.0 HB2 D:CYS272 3.2 81.8 1.0 CB D:CYS241 3.2 80.2 1.0 HA D:CYS272 3.2 81.8 1.0 H D:CYS244 3.2 82.4 1.0 CB D:CYS272 3.2 81.8 1.0 HB3 D:CYS241 3.3 80.2 1.0 HB3 D:CYS244 3.3 82.4 1.0 CB D:CYS244 3.4 82.4 1.0 HB3 D:CYS266 3.5 79.7 1.0 N D:CYS266 3.6 79.7 1.0 CA D:CYS272 3.7 81.8 1.0 CA D:CYS266 3.8 79.7 1.0 N D:CYS244 4.0 82.4 1.0 HB3 D:SER246 4.0 81.2 1.0 HB D:ILE243 4.0 81.7 1.0 HG D:SER249 4.0 78.2 1.0 HB3 D:CYS272 4.1 81.8 1.0 HB2 D:CYS244 4.2 82.4 1.0 CA D:CYS244 4.3 82.4 1.0 HA D:CYS266 4.3 79.7 1.0 H D:SER246 4.3 81.2 1.0 H D:ILE243 4.5 81.7 1.0 CA D:CYS241 4.6 80.2 1.0 HA D:VAL265 4.6 78.9 1.0 N D:CYS272 4.7 81.8 1.0 HD2 D:TYR271 4.7 79.1 1.0 H D:GLY245 4.8 82.1 1.0 HB2 D:SER246 4.8 81.2 1.0 C D:CYS272 4.8 81.8 1.0 H D:CYS272 4.8 81.8 1.0 CB D:SER246 4.8 81.2 1.0 OG D:SER249 4.8 78.2 1.0 HA D:CYS241 4.8 80.2 1.0 C D:VAL265 4.8 78.9 1.0 HB2 D:GLN275 4.8 82.0 1.0 O D:CYS272 4.9 81.8 1.0 C D:CYS244 4.9 82.4 1.0 HB D:VAL265 4.9 78.9 1.0 CB D:ILE243 4.9 81.7 1.0 O D:HOH422 5.0 80.1 1.0 C D:CYS266 5.0 79.7 1.0

Zinc binding site 3 out of 4 in the E. Coli C-P Lyase Bound to A Single Phnk Abc Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of E. Coli C-P Lyase Bound to A Single Phnk Abc Domain within 5.0Å range: probe atom residue distance (Å) B Occ G:Zn401 b:89.7 occ:0.54 NE2 G:HIS328 2.1 72.4 1.0 NE2 G:HIS333 2.1 71.4 1.0 CD2 G:HIS328 3.0 72.4 1.0 CE1 G:HIS328 3.1 72.4 1.0 CE1 G:HIS333 3.1 71.4 1.0 CD2 G:HIS333 3.1 71.4 1.0 HE1 H:HIS108 3.2 70.8 1.0 HD2 G:HIS328 3.2 72.4 1.0 HE1 G:HIS333 3.2 71.4 1.0 HE1 G:HIS328 3.3 72.4 1.0 HD2 G:HIS333 3.3 71.4 1.0 HG3 H:PRO126 3.4 73.0 1.0 HH21 H:ARG107 3.5 71.9 1.0 HE2 H:HIS108 3.8 70.8 1.0 CE1 H:HIS108 3.9 70.8 1.0 HB3 H:PRO126 4.1 73.0 1.0 ND1 G:HIS328 4.1 72.4 1.0 CG G:HIS328 4.2 72.4 1.0 ND1 G:HIS333 4.2 71.4 1.0 NE2 H:HIS108 4.2 70.8 1.0 CG G:HIS333 4.2 71.4 1.0 NH2 H:ARG107 4.3 71.9 1.0 CG H:PRO126 4.3 73.0 1.0 HG2 H:PRO187 4.3 72.4 1.0 HH22 H:ARG107 4.6 71.9 1.0 CB H:PRO126 4.6 73.0 1.0 HG2 H:PRO126 4.6 73.0 1.0 HE H:ARG107 4.6 71.9 1.0 O C:HOH603 4.7 77.8 1.0 HB2 H:PRO126 4.8 73.0 1.0 HD1 G:HIS328 4.9 72.4 1.0 HD1 G:HIS333 4.9 71.4 1.0

Zinc binding site 4 out of 4 in the E. Coli C-P Lyase Bound to A Single Phnk Abc Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of E. Coli C-P Lyase Bound to A Single Phnk Abc Domain within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn301 b:109.9 occ:1.00 SG H:CYS244 2.2 83.6 1.0 SG H:CYS272 2.3 81.8 1.0 SG H:CYS266 2.3 79.6 1.0 SG H:CYS241 2.3 79.6 1.0 HB2 H:CYS266 2.6 79.6 1.0 HB3 H:CYS244 2.9 83.6 1.0 H H:CYS266 2.9 79.6 1.0 H H:CYS244 3.0 83.6 1.0 CB H:CYS266 3.0 79.6 1.0 HA H:CYS272 3.1 81.8 1.0 CB H:CYS244 3.1 83.6 1.0 HB2 H:CYS272 3.2 81.8 1.0 CB H:CYS241 3.2 79.6 1.0 CB H:CYS272 3.2 81.8 1.0 HB2 H:CYS241 3.2 79.6 1.0 HB3 H:CYS241 3.2 79.6 1.0 CA H:CYS272 3.6 81.8 1.0 N H:CYS266 3.7 79.6 1.0 HB3 H:CYS266 3.7 79.6 1.0 N H:CYS244 3.7 83.6 1.0 HB H:ILE243 3.9 82.1 1.0 HB2 H:CYS244 3.9 83.6 1.0 CA H:CYS266 4.0 79.6 1.0 CA H:CYS244 4.0 83.6 1.0 HB3 H:SER246 4.0 80.7 1.0 HB3 H:CYS272 4.0 81.8 1.0 H H:SER246 4.1 80.7 1.0 HG H:SER249 4.2 78.8 1.0 H H:ILE243 4.4 82.1 1.0 H H:GLY245 4.4 80.7 1.0 HA H:CYS266 4.5 79.6 1.0 C H:CYS272 4.6 81.8 1.0 CA H:CYS241 4.6 79.6 1.0 O H:CYS272 4.6 81.8 1.0 HA H:VAL265 4.6 78.5 1.0 N H:CYS272 4.7 81.8 1.0 HB2 H:GLN275 4.7 83.4 1.0 C H:CYS244 4.7 83.6 1.0 HG21 H:ILE243 4.7 82.1 1.0 HD2 H:TYR271 4.7 80.2 1.0 N H:GLY245 4.8 80.7 1.0 CB H:ILE243 4.8 82.1 1.0 HA H:CYS244 4.8 83.6 1.0 CB H:SER246 4.9 80.7 1.0 HB2 H:SER246 4.9 80.7 1.0 H H:CYS272 4.9 81.8 1.0 C H:ILE243 4.9 82.1 1.0 C H:VAL265 4.9 78.5 1.0 HA H:CYS241 4.9 79.6 1.0 HB H:VAL265 4.9 78.5 1.0 OG H:SER249 5.0 78.8 1.0 N H:SER246 5.0 80.7 1.0

S.K.Amstrup, N.Sofos, J.L.Karlsen, R.B.Skjerning, T.Boesen, J.J.Enghild, B.Hove-Jensen, D.E.Brodersen. Structural Remodelling of the Carbon-Phosphorus Lyase Machinery By A Dual Abc Atpase Biorxiv 2022.
DOI: 10.1101/2022.06.09.495270