Zinc in PDB 7z18: E. Coli C-P Lyase Bound to A Phnk Abc Dimer and Atp

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

The structure of E. Coli C-P Lyase Bound to A Phnk Abc Dimer and Atp also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Zinc atom in the E. Coli C-P Lyase Bound to A Phnk Abc Dimer and Atp (pdb code 7z18). 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 and Atp, PDB code: 7z18:
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 and Atp


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 and Atp within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1000 b:69.9 occ:1.00 H111 D:I9X1001 1.6 5.0 1.0 NE2 C:HIS328 2.3 10.5 1.0 NE2 C:HIS333 2.3 10.5 1.0 O11 D:I9X1001 2.5 5.0 1.0 CD2 C:HIS333 3.0 10.5 1.0 HD2 C:HIS333 3.0 10.5 1.0 CE1 C:HIS328 3.2 10.5 1.0 CD2 C:HIS328 3.3 10.5 1.0 HE1 C:HIS328 3.4 10.5 1.0 CE1 C:HIS333 3.4 10.5 1.0 HD2 C:HIS328 3.4 10.5 1.0 O07 D:I9X1001 3.7 5.0 1.0 P08 D:I9X1001 3.7 5.0 1.0 HE1 C:HIS333 3.7 10.5 1.0 HD23 C:LEU329 3.8 5.8 1.0 HH21 D:ARG107 3.8 4.4 1.0 HE1 D:HIS108 3.9 5.3 1.0 CG C:HIS333 4.2 10.5 1.0 O09 D:I9X1001 4.3 5.0 1.0 ND1 C:HIS328 4.3 10.5 1.0 ND1 C:HIS333 4.4 10.5 1.0 CG C:HIS328 4.4 10.5 1.0 HG3 D:PRO126 4.4 4.9 1.0 NH2 D:ARG107 4.5 4.4 1.0 HH22 D:ARG107 4.6 4.4 1.0 CE1 D:HIS108 4.7 5.3 1.0 CD2 C:LEU329 4.7 5.8 1.0 HA C:LEU329 4.7 5.8 1.0 O10 D:I9X1001 4.7 5.0 1.0 C05 D:I9X1001 4.7 5.0 1.0 HD21 C:LEU329 4.8 5.8 1.0 H051 D:I9X1001 4.9 5.0 1.0 HB3 D:PRO126 4.9 4.9 1.0

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


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 and Atp within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1000 b:36.9 occ:1.00 SG D:CYS241 2.3 11.1 1.0 SG D:CYS244 2.3 12.9 1.0 SG D:CYS266 2.3 8.2 1.0 SG D:CYS272 2.3 11.3 1.0 HB2 D:CYS266 2.9 8.2 1.0 HB3 D:CYS241 3.0 11.1 1.0 H D:CYS266 3.0 8.2 1.0 CB D:CYS241 3.0 11.1 1.0 HB2 D:CYS241 3.1 11.1 1.0 H D:CYS244 3.2 12.9 1.0 CB D:CYS266 3.2 8.2 1.0 HB3 D:CYS244 3.2 12.9 1.0 HA D:CYS272 3.2 11.3 1.0 CB D:CYS244 3.4 12.9 1.0 CB D:CYS272 3.4 11.3 1.0 HB2 D:CYS272 3.5 11.3 1.0 N D:CYS266 3.8 8.2 1.0 HB D:ILE243 3.8 14.4 1.0 CA D:CYS272 3.8 11.3 1.0 N D:CYS244 3.8 12.9 1.0 HB3 D:CYS266 3.9 8.2 1.0 HB3 D:SER246 4.0 11.4 1.0 CA D:CYS266 4.1 8.2 1.0 H D:SER246 4.1 11.4 1.0 HB2 D:CYS244 4.1 12.9 1.0 CA D:CYS244 4.1 12.9 1.0 HG D:SER249 4.2 9.1 1.0 HB3 D:CYS272 4.3 11.3 1.0 H D:ILE243 4.3 14.4 1.0 H D:GLY245 4.4 11.1 1.0 CA D:CYS241 4.5 11.1 1.0 HA D:CYS266 4.5 8.2 1.0 HA D:VAL265 4.6 10.7 1.0 CB D:ILE243 4.7 14.4 1.0 HD2 D:TYR271 4.8 10.1 1.0 C D:CYS244 4.8 12.9 1.0 C D:CYS272 4.8 11.3 1.0 O D:CYS272 4.8 11.3 1.0 N D:GLY245 4.8 11.1 1.0 CB D:SER246 4.8 11.4 1.0 HB2 D:SER246 4.8 11.4 1.0 OG D:SER249 4.8 9.1 1.0 N D:CYS272 4.8 11.3 1.0 HB2 D:GLN275 4.9 17.1 1.0 C D:ILE243 4.9 14.4 1.0 HA D:CYS241 4.9 11.1 1.0 C D:VAL265 4.9 10.7 1.0 N D:SER246 4.9 11.4 1.0 HG22 D:ILE243 5.0 14.4 1.0 HA D:CYS244 5.0 12.9 1.0 HB D:VAL265 5.0 10.7 1.0

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


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 and Atp within 5.0Å range: probe atom residue distance (Å) B Occ G:Zn1000 b:71.8 occ:1.00 H111 H:I9X1001 1.6 5.1 1.0 NE2 G:HIS328 2.3 10.5 1.0 NE2 G:HIS333 2.3 10.5 1.0 O11 H:I9X1001 2.5 5.1 1.0 CD2 G:HIS333 3.0 10.5 1.0 HD2 G:HIS333 3.0 10.5 1.0 CE1 G:HIS328 3.2 10.5 1.0 CD2 G:HIS328 3.3 10.5 1.0 HE1 G:HIS328 3.4 10.5 1.0 CE1 G:HIS333 3.4 10.5 1.0 HD2 G:HIS328 3.4 10.5 1.0 O07 H:I9X1001 3.7 5.1 1.0 P08 H:I9X1001 3.7 5.1 1.0 HE1 G:HIS333 3.7 10.5 1.0 HD23 G:LEU329 3.8 5.7 1.0 HH21 H:ARG107 3.8 5.5 1.0 HE1 H:HIS108 3.9 6.3 1.0 CG G:HIS333 4.2 10.5 1.0 O09 H:I9X1001 4.3 5.1 1.0 ND1 G:HIS328 4.3 10.5 1.0 ND1 G:HIS333 4.4 10.5 1.0 CG G:HIS328 4.4 10.5 1.0 HG3 H:PRO126 4.4 5.4 1.0 NH2 H:ARG107 4.5 5.5 1.0 HH22 H:ARG107 4.6 5.5 1.0 HE2 H:HIS108 4.6 6.3 1.0 CE1 H:HIS108 4.7 6.3 1.0 CD2 G:LEU329 4.7 5.7 1.0 HA G:LEU329 4.7 5.7 1.0 O10 H:I9X1001 4.7 5.1 1.0 C05 H:I9X1001 4.7 5.1 1.0 HD21 G:LEU329 4.8 5.7 1.0 HB3 H:PRO126 4.9 5.4 1.0 H051 H:I9X1001 4.9 5.1 1.0

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


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 and Atp within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn1000 b:36.8 occ:1.00 SG H:CYS241 2.3 11.0 1.0 SG H:CYS244 2.3 12.8 1.0 SG H:CYS266 2.3 8.3 1.0 SG H:CYS272 2.3 11.2 1.0 HB2 H:CYS266 2.9 8.3 1.0 HB3 H:CYS241 3.0 11.0 1.0 H H:CYS266 3.0 8.3 1.0 CB H:CYS241 3.0 11.0 1.0 HB2 H:CYS241 3.1 11.0 1.0 H H:CYS244 3.2 12.8 1.0 CB H:CYS266 3.2 8.3 1.0 HB3 H:CYS244 3.2 12.8 1.0 HA H:CYS272 3.2 11.2 1.0 CB H:CYS244 3.4 12.8 1.0 CB H:CYS272 3.4 11.2 1.0 HB2 H:CYS272 3.5 11.2 1.0 N H:CYS266 3.8 8.3 1.0 HB H:ILE243 3.8 14.1 1.0 CA H:CYS272 3.8 11.2 1.0 N H:CYS244 3.8 12.8 1.0 HB3 H:CYS266 3.9 8.3 1.0 HB3 H:SER246 4.0 11.4 1.0 CA H:CYS266 4.1 8.3 1.0 H H:SER246 4.1 11.4 1.0 HB2 H:CYS244 4.1 12.8 1.0 CA H:CYS244 4.1 12.8 1.0 HG H:SER249 4.2 9.1 1.0 HB3 H:CYS272 4.3 11.2 1.0 H H:ILE243 4.3 14.1 1.0 H H:GLY245 4.4 11.0 1.0 CA H:CYS241 4.5 11.0 1.0 HA H:CYS266 4.5 8.3 1.0 HA H:VAL265 4.6 10.8 1.0 CB H:ILE243 4.7 14.1 1.0 HD2 H:TYR271 4.8 10.2 1.0 C H:CYS244 4.8 12.8 1.0 C H:CYS272 4.8 11.2 1.0 O H:CYS272 4.8 11.2 1.0 N H:GLY245 4.8 11.0 1.0 CB H:SER246 4.8 11.4 1.0 HB2 H:SER246 4.8 11.4 1.0 OG H:SER249 4.8 9.1 1.0 N H:CYS272 4.8 11.2 1.0 HB2 H:GLN275 4.9 16.9 1.0 C H:ILE243 4.9 14.1 1.0 HA H:CYS241 4.9 11.0 1.0 C H:VAL265 4.9 10.8 1.0 N H:SER246 4.9 11.4 1.0 HG22 H:ILE243 5.0 14.1 1.0 HA H:CYS244 5.0 12.8 1.0 HB H:VAL265 5.0 10.8 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.
ISSN: ISSN 2692-8205
DOI: 10.1101/2022.06.09.495270