Magnesium 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:

Zinc

(Zn)

4 atoms

The binding sites of Magnesium 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 Magnesium atom.
In total 2 binding sites of Magnesium where determined in the E. Coli C-P Lyase Bound to A Phnk Abc Dimer and Atp, PDB code: 7z18:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 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 Magnesium with other atoms in the Mg 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 I:Mg1001 b:33.9 occ:1.00 OG1 I:THR45 1.9 42.0 1.0 HG1 I:THR45 2.2 42.0 1.0 OE1 I:GLN90 2.3 41.5 1.0 O2G I:ATP1000 2.3 44.4 1.0 O2B I:ATP1000 2.4 44.4 1.0 O I:HOH1101 2.8 39.0 1.0 O3B I:ATP1000 3.0 44.4 1.0 H2 I:HOH1101 3.0 39.0 1.0 PG I:ATP1000 3.1 44.4 1.0 H1 I:HOH1101 3.2 39.0 1.0 CD I:GLN90 3.2 41.5 1.0 HE22 I:GLN90 3.3 41.5 1.0 CB I:THR45 3.3 42.0 1.0 PB I:ATP1000 3.3 44.4 1.0 HB I:THR45 3.4 42.0 1.0 O1G I:ATP1000 3.6 44.4 1.0 NE2 I:GLN90 3.6 41.5 1.0 H I:THR45 3.7 42.0 1.0 HB2 J:SER147 3.7 40.7 1.0 OD2 I:ASP170 3.8 43.2 1.0 HG21 I:THR45 3.8 42.0 1.0 H J:GLY148 3.9 39.9 1.0 O1A I:ATP1000 4.0 44.4 1.0 CG2 I:THR45 4.1 42.0 1.0 O3A I:ATP1000 4.1 44.4 1.0 OD1 I:ASP170 4.2 43.2 1.0 N I:THR45 4.2 42.0 1.0 CA I:THR45 4.2 42.0 1.0 CG I:ASP170 4.3 43.2 1.0 HG23 I:THR45 4.4 42.0 1.0 HA I:THR45 4.4 42.0 1.0 HE21 I:GLN90 4.4 41.5 1.0 O1B I:ATP1000 4.4 44.4 1.0 O3G I:ATP1000 4.4 44.4 1.0 HB2 I:LYS44 4.5 44.5 1.0 HB2 I:GLN90 4.5 41.5 1.0 CG I:GLN90 4.5 41.5 1.0 PA I:ATP1000 4.6 44.4 1.0 CB J:SER147 4.6 40.7 1.0 HE2 I:LYS44 4.7 44.5 1.0 N J:GLY148 4.7 39.9 1.0 HG3 I:GLN90 4.7 41.5 1.0 HG11 I:VAL202 4.8 43.9 1.0 HB3 J:SER147 4.8 40.7 1.0 H J:GLY149 4.9 40.6 1.0 HG3 I:GLU171 4.9 44.3 1.0 HG22 I:THR45 4.9 42.0 1.0 CB I:GLN90 5.0 41.5 1.0 HA3 J:GLY148 5.0 39.9 1.0

Magnesium binding site 2 out of 2 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 Magnesium with other atoms in the Mg 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 J:Mg1001 b:34.5 occ:1.00 OG1 J:THR45 1.9 42.1 1.0 HG1 J:THR45 2.2 42.1 1.0 OE1 J:GLN90 2.3 41.6 1.0 O2G J:ATP1000 2.3 44.5 1.0 O2B J:ATP1000 2.3 44.5 1.0 O J:HOH1101 2.8 39.0 1.0 H2 J:HOH1101 2.9 39.0 1.0 O3B J:ATP1000 3.0 44.5 1.0 PG J:ATP1000 3.1 44.5 1.0 H1 J:HOH1101 3.2 39.0 1.0 CD J:GLN90 3.2 41.6 1.0 HE22 J:GLN90 3.3 41.6 1.0 CB J:THR45 3.3 42.1 1.0 PB J:ATP1000 3.3 44.5 1.0 HB J:THR45 3.4 42.1 1.0 O1G J:ATP1000 3.6 44.5 1.0 NE2 J:GLN90 3.6 41.6 1.0 H J:THR45 3.7 42.1 1.0 HB2 I:SER147 3.7 40.9 1.0 OD2 J:ASP170 3.8 43.4 1.0 HG21 J:THR45 3.8 42.1 1.0 H I:GLY148 3.9 40.1 1.0 O1A J:ATP1000 4.0 44.5 1.0 CG2 J:THR45 4.1 42.1 1.0 O3A J:ATP1000 4.1 44.5 1.0 OD1 J:ASP170 4.2 43.4 1.0 N J:THR45 4.2 42.1 1.0 CA J:THR45 4.3 42.1 1.0 CG J:ASP170 4.3 43.4 1.0 HG23 J:THR45 4.4 42.1 1.0 HA J:THR45 4.4 42.1 1.0 HE21 J:GLN90 4.4 41.6 1.0 O1B J:ATP1000 4.4 44.5 1.0 O3G J:ATP1000 4.4 44.5 1.0 HB2 J:LYS44 4.5 44.5 1.0 HB2 J:GLN90 4.5 41.6 1.0 CG J:GLN90 4.5 41.6 1.0 PA J:ATP1000 4.6 44.5 1.0 CB I:SER147 4.6 40.9 1.0 HE2 J:LYS44 4.7 44.5 1.0 N I:GLY148 4.7 40.1 1.0 HG3 J:GLN90 4.7 41.6 1.0 HG11 J:VAL202 4.8 43.9 1.0 HB3 I:SER147 4.8 40.9 1.0 H I:GLY149 4.9 40.8 1.0 HG3 J:GLU171 4.9 44.3 1.0 HG22 J:THR45 4.9 42.1 1.0 CB J:GLN90 5.0 41.6 1.0 HA3 I:GLY148 5.0 40.1 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.
ISSN: ISSN 2692-8205
DOI: 10.1101/2022.06.09.495270