Zinc in PDB 7z15: E. Coli C-P Lyase Bound to A Phnk/Phnl Dual Abc Dimer and Adp + Pi

All present enzymatic activity of E. Coli C-P Lyase Bound to A Phnk/Phnl Dual Abc Dimer and Adp + Pi:
2.7.8.37; 4.7.1.1;

The structure of E. Coli C-P Lyase Bound to A Phnk/Phnl Dual Abc Dimer and Adp + Pi also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Zinc atom in the E. Coli C-P Lyase Bound to A Phnk/Phnl Dual Abc Dimer and Adp + Pi (pdb code 7z15). 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 Phnk/Phnl Dual Abc Dimer and Adp + Pi, PDB code: 7z15:
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 Phnk/Phnl Dual Abc Dimer and Adp + Pi


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 Phnk/Phnl Dual Abc Dimer and Adp + Pi within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1000 b:55.3 occ:1.00 NE2 C:HIS333 2.1 9.7 1.0 NE2 C:HIS328 2.1 9.3 1.0 O09 D:I9X1001 2.2 11.4 1.0 O C:HOH1264 2.3 11.8 1.0 O C:HOH1266 2.3 16.9 1.0 O D:HOH1256 2.5 16.6 1.0 CD2 C:HIS328 2.9 9.3 1.0 CD2 C:HIS333 2.9 9.7 1.0 HD2 C:HIS328 3.0 9.3 1.0 HD2 C:HIS333 3.1 9.7 1.0 CE1 C:HIS333 3.1 9.7 1.0 CE1 C:HIS328 3.2 9.3 1.0 P08 D:I9X1001 3.3 11.4 1.0 O07 D:I9X1001 3.4 11.4 1.0 HE1 C:HIS333 3.4 9.7 1.0 HH21 D:ARG107 3.5 7.3 1.0 HE1 C:HIS328 3.5 9.3 1.0 H111 D:I9X1001 3.6 11.4 1.0 HE1 D:HIS108 3.7 7.5 1.0 HD23 C:LEU329 3.9 10.4 1.0 O11 D:I9X1001 4.0 11.4 1.0 CG C:HIS328 4.1 9.3 1.0 CG C:HIS333 4.1 9.7 1.0 ND1 C:HIS333 4.2 9.7 1.0 O G:HOH1279 4.2 8.6 1.0 NH2 D:ARG107 4.2 7.3 1.0 ND1 C:HIS328 4.2 9.3 1.0 O D:HOH1171 4.3 16.9 1.0 O10 D:I9X1001 4.3 11.4 1.0 HG3 D:PRO126 4.4 10.8 1.0 HH22 D:ARG107 4.4 7.3 1.0 C05 D:I9X1001 4.4 11.4 1.0 CE1 D:HIS108 4.5 7.5 1.0 H051 D:I9X1001 4.5 11.4 1.0 HA C:LEU329 4.7 10.4 1.0 HE1 C:PHE325 4.7 17.8 1.0 HB3 D:PRO126 4.7 10.8 1.0 CD2 C:LEU329 4.8 10.4 1.0 HD21 C:LEU329 4.8 10.4 1.0 O G:HOH1251 4.9 11.8 1.0 NE2 D:HIS108 4.9 7.5 1.0 HD1 C:HIS333 5.0 9.7 1.0 C04 D:I9X1001 5.0 11.4 1.0 HE D:ARG107 5.0 7.3 1.0

Zinc binding site 2 out of 4 in the E. Coli C-P Lyase Bound to A Phnk/Phnl Dual Abc Dimer and Adp + Pi


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 Phnk/Phnl Dual Abc Dimer and Adp + Pi within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1000 b:35.3 occ:1.00 SG D:CYS241 2.3 19.2 1.0 SG D:CYS244 2.3 21.5 1.0 SG D:CYS266 2.3 15.7 1.0 SG D:CYS272 2.3 18.3 1.0 H D:CYS244 2.9 21.5 1.0 HB2 D:CYS241 3.0 19.2 1.0 HB3 D:CYS244 3.0 21.5 1.0 HB3 D:CYS241 3.0 19.2 1.0 CB D:CYS241 3.0 19.2 1.0 H D:CYS266 3.1 15.7 1.0 HB2 D:CYS266 3.1 15.7 1.0 HA D:CYS272 3.2 18.3 1.0 CB D:CYS244 3.2 21.5 1.0 CB D:CYS266 3.3 15.7 1.0 CB D:CYS272 3.4 18.3 1.0 HB2 D:CYS272 3.4 18.3 1.0 N D:CYS244 3.7 21.5 1.0 HB D:ILE243 3.8 22.0 1.0 CA D:CYS272 3.8 18.3 1.0 HB3 D:SER246 3.8 19.3 1.0 N D:CYS266 3.9 15.7 1.0 H D:SER246 4.0 19.3 1.0 CA D:CYS244 4.0 21.5 1.0 HB2 D:CYS244 4.0 21.5 1.0 HB3 D:CYS266 4.1 15.7 1.0 HG D:SER249 4.2 14.9 1.0 CA D:CYS266 4.2 15.7 1.0 HB3 D:CYS272 4.2 18.3 1.0 H D:ILE243 4.3 22.0 1.0 H D:GLY245 4.3 20.1 1.0 CA D:CYS241 4.5 19.2 1.0 O D:HOH1224 4.6 17.9 1.0 HB2 D:GLN275 4.6 23.9 1.0 HA D:VAL265 4.6 17.1 1.0 C D:CYS244 4.6 21.5 1.0 HD2 D:TYR271 4.6 17.8 1.0 N D:GLY245 4.7 20.1 1.0 CB D:SER246 4.7 19.3 1.0 HA D:CYS266 4.7 15.7 1.0 O D:CYS272 4.7 18.3 1.0 CB D:ILE243 4.7 22.0 1.0 HE2 D:TYR271 4.7 17.8 1.0 C D:CYS272 4.7 18.3 1.0 HB2 D:SER246 4.8 19.3 1.0 C D:ILE243 4.8 22.0 1.0 N D:SER246 4.8 19.3 1.0 HA D:CYS244 4.8 21.5 1.0 HA D:CYS241 4.8 19.2 1.0 N D:CYS272 4.8 18.3 1.0 HG22 D:ILE243 4.9 22.0 1.0

Zinc binding site 3 out of 4 in the E. Coli C-P Lyase Bound to A Phnk/Phnl Dual Abc Dimer and Adp + Pi


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 Phnk/Phnl Dual Abc Dimer and Adp + Pi within 5.0Å range: probe atom residue distance (Å) B Occ G:Zn1000 b:56.8 occ:1.00 NE2 G:HIS333 2.1 9.4 1.0 NE2 G:HIS328 2.1 9.6 1.0 O09 H:I9X1001 2.2 10.3 1.0 O G:HOH1266 2.3 10.9 1.0 O G:HOH1267 2.3 17.2 1.0 O G:HOH1263 2.8 15.5 1.0 CD2 G:HIS328 2.9 9.6 1.0 CD2 G:HIS333 2.9 9.4 1.0 HD2 G:HIS328 3.0 9.6 1.0 HD2 G:HIS333 3.1 9.4 1.0 CE1 G:HIS333 3.1 9.4 1.0 CE1 G:HIS328 3.2 9.6 1.0 P08 H:I9X1001 3.2 10.3 1.0 O07 H:I9X1001 3.4 10.3 1.0 HE1 G:HIS333 3.4 9.4 1.0 HH21 H:ARG107 3.5 7.1 1.0 HE1 G:HIS328 3.5 9.6 1.0 H111 H:I9X1001 3.6 10.3 1.0 HE1 H:HIS108 3.7 7.5 1.0 HD23 G:LEU329 3.9 10.3 1.0 O11 H:I9X1001 4.0 10.3 1.0 CG G:HIS328 4.1 9.6 1.0 CG G:HIS333 4.1 9.4 1.0 ND1 G:HIS333 4.2 9.4 1.0 O C:HOH1250 4.2 8.4 1.0 NH2 H:ARG107 4.2 7.1 1.0 ND1 G:HIS328 4.2 9.6 1.0 O H:HOH1167 4.3 16.4 1.0 O10 H:I9X1001 4.3 10.3 1.0 HG3 H:PRO126 4.4 10.9 1.0 HH22 H:ARG107 4.4 7.1 1.0 C05 H:I9X1001 4.4 10.3 1.0 CE1 H:HIS108 4.5 7.5 1.0 H051 H:I9X1001 4.5 10.3 1.0 HA G:LEU329 4.7 10.3 1.0 HE1 G:PHE325 4.7 17.8 1.0 HB3 H:PRO126 4.7 10.9 1.0 CD2 G:LEU329 4.8 10.3 1.0 HD21 G:LEU329 4.8 10.3 1.0 O C:HOH1253 4.9 11.6 1.0 NE2 H:HIS108 4.9 7.5 1.0 HD1 G:HIS333 5.0 9.4 1.0 C04 H:I9X1001 5.0 10.3 1.0 HE H:ARG107 5.0 7.1 1.0

Zinc binding site 4 out of 4 in the E. Coli C-P Lyase Bound to A Phnk/Phnl Dual Abc Dimer and Adp + Pi


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 Phnk/Phnl Dual Abc Dimer and Adp + Pi within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn1000 b:36.2 occ:1.00 SG H:CYS241 2.3 19.2 1.0 SG H:CYS244 2.3 21.7 1.0 SG H:CYS266 2.3 15.7 1.0 SG H:CYS272 2.3 18.3 1.0 H H:CYS244 2.9 21.7 1.0 HB2 H:CYS241 3.0 19.2 1.0 HB3 H:CYS244 3.0 21.7 1.0 HB3 H:CYS241 3.0 19.2 1.0 CB H:CYS241 3.0 19.2 1.0 H H:CYS266 3.1 15.7 1.0 HB2 H:CYS266 3.1 15.7 1.0 HA H:CYS272 3.2 18.3 1.0 CB H:CYS244 3.2 21.7 1.0 CB H:CYS266 3.3 15.7 1.0 CB H:CYS272 3.4 18.3 1.0 HB2 H:CYS272 3.4 18.3 1.0 N H:CYS244 3.7 21.7 1.0 HB H:ILE243 3.8 22.2 1.0 CA H:CYS272 3.8 18.3 1.0 HB3 H:SER246 3.8 19.1 1.0 N H:CYS266 3.9 15.7 1.0 CA H:CYS244 4.0 21.7 1.0 H H:SER246 4.0 19.1 1.0 HB2 H:CYS244 4.0 21.7 1.0 HB3 H:CYS266 4.1 15.7 1.0 HG H:SER249 4.2 14.9 1.0 CA H:CYS266 4.2 15.7 1.0 HB3 H:CYS272 4.2 18.3 1.0 H H:ILE243 4.3 22.2 1.0 H H:GLY245 4.3 20.3 1.0 CA H:CYS241 4.5 19.2 1.0 O H:HOH1220 4.6 18.0 1.0 HB2 H:GLN275 4.6 24.0 1.0 HA H:VAL265 4.6 17.2 1.0 C H:CYS244 4.6 21.7 1.0 HD2 H:TYR271 4.6 17.8 1.0 N H:GLY245 4.7 20.3 1.0 CB H:SER246 4.7 19.1 1.0 HA H:CYS266 4.7 15.7 1.0 CB H:ILE243 4.7 22.2 1.0 O H:CYS272 4.7 18.3 1.0 HE2 H:TYR271 4.7 17.8 1.0 C H:CYS272 4.7 18.3 1.0 HB2 H:SER246 4.8 19.1 1.0 C H:ILE243 4.8 22.2 1.0 N H:SER246 4.8 19.1 1.0 HA H:CYS244 4.8 21.7 1.0 HA H:CYS241 4.8 19.2 1.0 N H:CYS272 4.8 18.3 1.0 HG22 H:ILE243 4.9 22.2 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