Zinc in PDB 7z17: E. Coli C-P Lyase Bound to A Phnk Abc Dimer in An Open Conformation

All present enzymatic activity of E. Coli C-P Lyase Bound to A Phnk Abc Dimer in An Open Conformation:
2.7.8.37; 4.7.1.1;

The binding sites of Zinc atom in the E. Coli C-P Lyase Bound to A Phnk Abc Dimer in An Open Conformation (pdb code 7z17). 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 Abc Dimer in An Open Conformation, PDB code: 7z17:
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 Abc Dimer in An Open Conformation


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 Abc Dimer in An Open Conformation within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1000 b:94.3 occ:1.00 H111 D:I9X1001 1.8 6.2 1.0 O11 D:I9X1001 2.4 6.2 1.0 NE2 C:HIS333 2.4 6.2 1.0 NE2 C:HIS328 2.5 6.2 1.0 HD2 C:HIS333 2.7 6.2 1.0 CD2 C:HIS333 2.9 6.2 1.0 CD2 C:HIS328 3.4 6.2 1.0 CE1 C:HIS328 3.4 6.2 1.0 HD2 C:HIS328 3.5 6.2 1.0 HE1 C:HIS328 3.6 6.2 1.0 CE1 C:HIS333 3.6 6.2 1.0 P08 D:I9X1001 3.6 6.2 1.0 O07 D:I9X1001 3.7 6.2 1.0 HE1 D:HIS108 3.9 6.2 1.0 HH21 D:ARG107 3.9 6.2 1.0 HD23 C:LEU329 3.9 6.2 1.0 HE1 C:HIS333 4.0 6.2 1.0 CG C:HIS333 4.1 6.2 1.0 O09 D:I9X1001 4.4 6.2 1.0 HG3 D:PRO126 4.4 6.2 1.0 NH2 D:ARG107 4.4 6.2 1.0 HH22 D:ARG107 4.4 6.2 1.0 ND1 C:HIS333 4.5 6.2 1.0 ND1 C:HIS328 4.5 6.2 1.0 CG C:HIS328 4.5 6.2 1.0 O10 D:I9X1001 4.6 6.2 1.0 CE1 D:HIS108 4.6 6.2 1.0 CD2 C:LEU329 4.7 6.2 1.0 C05 D:I9X1001 4.7 6.2 1.0 HA C:LEU329 4.8 6.2 1.0 HE2 D:HIS108 4.8 6.2 1.0 HD21 C:LEU329 4.8 6.2 1.0 H051 D:I9X1001 4.9 6.2 1.0 HB3 D:PRO126 4.9 6.2 1.0 HD22 C:LEU329 5.0 6.2 1.0

Zinc binding site 2 out of 4 in the E. Coli C-P Lyase Bound to A Phnk Abc Dimer in An Open Conformation


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 Abc Dimer in An Open Conformation within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1000 b:70.7 occ:1.00 SG D:CYS241 2.3 9.6 1.0 SG D:CYS272 2.3 17.1 1.0 SG D:CYS244 2.3 15.6 1.0 SG D:CYS266 2.3 7.8 1.0 HB2 D:CYS241 3.0 9.6 1.0 CB D:CYS241 3.0 9.6 1.0 H D:CYS244 3.1 15.6 1.0 H D:CYS266 3.1 7.8 1.0 HB3 D:CYS241 3.1 9.6 1.0 HB2 D:CYS266 3.1 7.8 1.0 HA D:CYS272 3.2 17.1 1.0 HB2 D:CYS272 3.3 17.1 1.0 CB D:CYS272 3.3 17.1 1.0 CB D:CYS266 3.3 7.8 1.0 HB3 D:CYS244 3.6 15.6 1.0 CB D:CYS244 3.6 15.6 1.0 HB3 D:SER246 3.6 12.8 1.0 HB D:ILE243 3.7 15.5 1.0 CA D:CYS272 3.8 17.1 1.0 N D:CYS244 3.8 15.6 1.0 N D:CYS266 3.8 7.8 1.0 HG D:SER249 3.9 8.3 1.0 HB3 D:CYS266 4.1 7.8 1.0 H D:SER246 4.1 12.8 1.0 HB3 D:CYS272 4.2 17.1 1.0 CA D:CYS266 4.2 7.8 1.0 HB2 D:SER246 4.2 12.8 1.0 H D:ILE243 4.3 15.5 1.0 CA D:CYS244 4.3 15.6 1.0 HB2 D:CYS244 4.4 15.6 1.0 CB D:SER246 4.4 12.8 1.0 HG22 D:ILE243 4.4 15.5 1.0 HA D:VAL265 4.5 8.6 1.0 CA D:CYS241 4.5 9.6 1.0 CB D:ILE243 4.6 15.5 1.0 HA D:CYS266 4.7 7.8 1.0 O D:CYS272 4.7 17.1 1.0 OG D:SER249 4.7 8.3 1.0 C D:CYS272 4.7 17.1 1.0 HB2 D:GLN275 4.8 20.5 1.0 HA D:CYS241 4.8 9.6 1.0 N D:CYS272 4.9 17.1 1.0 H D:GLY245 4.9 10.1 1.0 C D:CYS244 4.9 15.6 1.0 C D:ILE243 4.9 15.5 1.0 HD21 D:LEU251 4.9 4.9 1.0 N D:SER246 4.9 12.8 1.0 HD2 D:TYR271 4.9 12.6 1.0 HD23 D:LEU251 5.0 4.9 1.0 HG12 D:VAL265 5.0 8.6 1.0 HD12 D:ILE243 5.0 15.5 1.0 C D:VAL265 5.0 8.6 1.0 CG2 D:ILE243 5.0 15.5 1.0 N D:ILE243 5.0 15.5 1.0

Zinc binding site 3 out of 4 in the E. Coli C-P Lyase Bound to A Phnk Abc Dimer in An Open Conformation


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 Abc Dimer in An Open Conformation within 5.0Å range: probe atom residue distance (Å) B Occ G:Zn1000 b:84.9 occ:1.00 NE2 C:HIS219 2.0 17.7 1.0 NE2 G:HIS333 2.1 12.2 1.0 NE2 G:HIS328 2.1 9.7 1.0 N G:MET1 2.1 40.4 1.0 H2 G:MET1 2.5 40.4 1.0 H3 G:MET1 2.6 40.4 1.0 HD2 G:HIS333 2.7 12.2 1.0 CD2 G:HIS333 2.7 12.2 1.0 CE1 G:HIS328 2.9 9.7 1.0 CA G:MET1 2.9 40.4 1.0 HA G:MET1 2.9 40.4 1.0 CE1 C:HIS219 3.0 17.7 1.0 HE1 G:HIS328 3.0 9.7 1.0 CD2 C:HIS219 3.0 17.7 1.0 CD2 G:HIS328 3.1 9.7 1.0 HE1 C:HIS219 3.2 17.7 1.0 CE1 G:HIS333 3.2 12.2 1.0 HD2 C:HIS219 3.2 17.7 1.0 C G:MET1 3.3 40.4 1.0 HD2 G:HIS328 3.3 9.7 1.0 O G:MET1 3.5 40.4 1.0 HE1 G:HIS333 3.6 12.2 1.0 CG G:HIS333 3.9 12.2 1.0 ND1 G:HIS328 3.9 9.7 1.0 N G:TYR2 4.1 27.1 1.0 CG G:HIS328 4.1 9.7 1.0 ND1 C:HIS219 4.1 17.7 1.0 ND1 G:HIS333 4.1 12.2 1.0 CG C:HIS219 4.2 17.7 1.0 CB G:MET1 4.3 40.4 1.0 H G:TYR2 4.3 27.1 1.0 OD2 G:ASP336 4.4 16.8 1.0 HG23 G:VAL3 4.4 22.3 1.0 HB2 G:MET1 4.5 40.4 1.0 HE1 C:PHE221 4.6 10.3 1.0 HB3 G:MET1 4.7 40.4 1.0 HD1 G:HIS328 4.7 9.7 1.0 HA G:TYR2 4.7 27.1 1.0 HD1 C:HIS219 4.9 17.7 1.0 HD1 G:HIS333 5.0 12.2 1.0 CA G:TYR2 5.0 27.1 1.0 HD12 G:LEU329 5.0 6.4 1.0

Zinc binding site 4 out of 4 in the E. Coli C-P Lyase Bound to A Phnk Abc Dimer in An Open Conformation


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 Abc Dimer in An Open Conformation within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn1000 b:137.7 occ:1.00 SG H:CYS241 2.3 77.3 1.0 SG H:CYS244 2.3 78.8 1.0 SG H:CYS266 2.3 68.0 1.0 SG H:CYS272 2.3 66.0 1.0 HB2 H:CYS266 2.9 68.0 1.0 H H:CYS266 2.9 68.0 1.0 HB3 H:CYS241 3.0 77.3 1.0 CB H:CYS241 3.0 77.3 1.0 HB2 H:CYS241 3.1 77.3 1.0 H H:CYS244 3.1 78.8 1.0 CB H:CYS266 3.2 68.0 1.0 HA H:CYS272 3.4 66.0 1.0 CB H:CYS272 3.6 66.0 1.0 HB H:ILE243 3.6 73.1 1.0 HE21 H:GLN275 3.7 70.0 1.0 HB2 H:CYS272 3.7 66.0 1.0 N H:CYS266 3.7 68.0 1.0 CB H:CYS244 3.7 78.8 1.0 HB3 H:CYS244 3.8 78.8 1.0 N H:CYS244 3.9 78.8 1.0 HE22 H:GLN275 3.9 70.0 1.0 HB3 H:CYS266 3.9 68.0 1.0 CA H:CYS272 4.0 66.0 1.0 CA H:CYS266 4.1 68.0 1.0 NE2 H:GLN275 4.1 70.0 1.0 H H:ILE243 4.2 73.1 1.0 H H:GLY245 4.2 81.6 1.0 CA H:CYS244 4.4 78.8 1.0 HB3 H:CYS272 4.4 66.0 1.0 HB2 H:CYS244 4.5 78.8 1.0 HA H:VAL265 4.5 57.1 1.0 CA H:CYS241 4.5 77.3 1.0 HA H:CYS266 4.5 68.0 1.0 CB H:ILE243 4.6 73.1 1.0 HG H:SER249 4.6 64.9 1.0 HD12 H:ILE243 4.7 73.1 1.0 N H:GLY245 4.7 81.6 1.0 O H:CYS272 4.8 66.0 1.0 HD21 H:LEU251 4.8 62.8 1.0 C H:CYS272 4.9 66.0 1.0 C H:VAL265 4.9 57.1 1.0 HB2 H:GLN275 4.9 70.0 1.0 HA H:CYS241 4.9 77.3 1.0 O H:SER246 4.9 76.8 1.0 HB H:VAL265 4.9 57.1 1.0 C H:CYS244 4.9 78.8 1.0 N H:ILE243 4.9 73.1 1.0 C H:ILE243 5.0 73.1 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