Magnesium in PDB 7z16: E. Coli C-P Lyase Bound to Phnk/Phnl Dual Abc Dimer with Amppnp and Phnk E171Q Mutation

All present enzymatic activity of E. Coli C-P Lyase Bound to Phnk/Phnl Dual Abc Dimer with Amppnp and Phnk E171Q Mutation:
2.7.8.37; 4.7.1.1;

The structure of E. Coli C-P Lyase Bound to Phnk/Phnl Dual Abc Dimer with Amppnp and Phnk E171Q Mutation 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 Phnk/Phnl Dual Abc Dimer with Amppnp and Phnk E171Q Mutation (pdb code 7z16). 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 Phnk/Phnl Dual Abc Dimer with Amppnp and Phnk E171Q Mutation, PDB code: 7z16:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the E. Coli C-P Lyase Bound to Phnk/Phnl Dual Abc Dimer with Amppnp and Phnk E171Q Mutation


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 Phnk/Phnl Dual Abc Dimer with Amppnp and Phnk E171Q Mutation within 5.0Å range: probe atom residue distance (Å) B Occ I:Mg1001 b:39.1 occ:1.00 H1 I:HOH1101 1.6 36.0 1.0 H1 I:HOH1103 1.6 37.3 1.0 OG1 I:THR45 2.0 37.8 1.0 O2G I:ANP1002 2.1 38.1 1.0 O2B I:ANP1002 2.2 38.1 1.0 O I:HOH1101 2.3 36.0 1.0 HG1 I:THR45 2.4 37.8 1.0 O I:HOH1103 2.5 37.3 1.0 H2 I:HOH1103 2.7 37.3 1.0 H2 I:HOH1101 2.9 36.0 1.0 PG I:ANP1002 3.1 38.1 1.0 CB I:THR45 3.2 37.8 1.0 HB I:THR45 3.3 37.8 1.0 PB I:ANP1002 3.3 38.1 1.0 H1 I:HOH1102 3.4 35.6 1.0 H I:THR45 3.5 37.8 1.0 O3G I:ANP1002 3.5 38.1 1.0 N3B I:ANP1002 3.6 38.1 1.0 OE1 I:GLN90 3.6 34.5 1.0 OD2 I:ASP170 3.7 36.0 1.0 HB2 J:SER147 3.8 36.5 1.0 H J:GLY148 3.9 35.7 1.0 HG21 I:THR45 3.9 37.8 1.0 O2A I:ANP1002 4.0 38.1 1.0 N I:THR45 4.0 37.8 1.0 OD1 I:ASP170 4.1 36.0 1.0 CA I:THR45 4.1 37.8 1.0 CG2 I:THR45 4.2 37.8 1.0 NE2 I:GLN171 4.2 36.8 1.0 O I:HOH1102 4.2 35.6 1.0 HB2 I:LYS44 4.2 39.6 1.0 O3A I:ANP1002 4.3 38.1 1.0 CG I:ASP170 4.3 36.0 1.0 HA I:THR45 4.4 37.8 1.0 HNB1 I:ANP1002 4.4 38.1 1.0 O1G I:ANP1002 4.4 38.1 1.0 O1B I:ANP1002 4.5 38.1 1.0 HE2 I:LYS44 4.6 39.6 1.0 HZ3 I:LYS44 4.6 39.6 1.0 PA I:ANP1002 4.6 38.1 1.0 HG23 I:THR45 4.6 37.8 1.0 H2 I:HOH1102 4.7 35.6 1.0 HG11 I:VAL202 4.7 38.5 1.0 CD I:GLN90 4.7 34.5 1.0 N J:GLY148 4.7 35.7 1.0 CB J:SER147 4.8 36.5 1.0 O1A I:ANP1002 4.8 38.1 1.0 HG22 I:THR45 4.9 37.8 1.0 HA3 J:GLY148 5.0 35.7 1.0

Magnesium binding site 2 out of 2 in the E. Coli C-P Lyase Bound to Phnk/Phnl Dual Abc Dimer with Amppnp and Phnk E171Q Mutation


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 Phnk/Phnl Dual Abc Dimer with Amppnp and Phnk E171Q Mutation within 5.0Å range: probe atom residue distance (Å) B Occ J:Mg1001 b:39.1 occ:1.00 H1 J:HOH1103 1.7 37.3 1.0 H2 J:HOH1101 1.8 36.0 1.0 OG1 J:THR45 2.0 37.8 1.0 O J:HOH1101 2.0 36.0 1.0 O2G J:ANP1002 2.1 38.1 1.0 O2B J:ANP1002 2.2 38.1 1.0 HG1 J:THR45 2.4 37.8 1.0 O J:HOH1103 2.5 37.3 1.0 H2 J:HOH1103 2.7 37.3 1.0 H1 J:HOH1101 2.8 36.0 1.0 PG J:ANP1002 3.1 38.1 1.0 CB J:THR45 3.2 37.8 1.0 HB J:THR45 3.3 37.8 1.0 PB J:ANP1002 3.3 38.1 1.0 H2 J:HOH1102 3.4 35.6 1.0 H J:THR45 3.5 37.8 1.0 O3G J:ANP1002 3.5 38.1 1.0 N3B J:ANP1002 3.6 38.1 1.0 OE1 J:GLN90 3.6 34.5 1.0 OD2 J:ASP170 3.7 36.0 1.0 HB2 I:SER147 3.8 36.5 1.0 H I:GLY148 3.9 35.7 1.0 HG23 J:THR45 3.9 37.8 1.0 O2A J:ANP1002 4.0 38.1 1.0 N J:THR45 4.0 37.8 1.0 OD1 J:ASP170 4.1 36.0 1.0 CA J:THR45 4.1 37.8 1.0 CG2 J:THR45 4.2 37.8 1.0 NE2 J:GLN171 4.2 36.8 1.0 HB2 J:LYS44 4.2 39.6 1.0 O J:HOH1102 4.2 35.6 1.0 O3A J:ANP1002 4.3 38.1 1.0 CG J:ASP170 4.3 36.0 1.0 HA J:THR45 4.4 37.8 1.0 HNB1 J:ANP1002 4.4 38.1 1.0 O1G J:ANP1002 4.4 38.1 1.0 O1B J:ANP1002 4.5 38.1 1.0 HE2 J:LYS44 4.6 39.6 1.0 PA J:ANP1002 4.6 38.1 1.0 HG22 J:THR45 4.6 37.8 1.0 H1 J:HOH1102 4.7 35.6 1.0 HG11 J:VAL202 4.7 38.5 1.0 CD J:GLN90 4.7 34.5 1.0 N I:GLY148 4.7 35.7 1.0 CB I:SER147 4.8 36.5 1.0 HZ1 J:LYS44 4.8 39.6 1.0 O1A J:ANP1002 4.8 38.1 1.0 HG21 J:THR45 4.9 37.8 1.0 HZ3 J:LYS44 4.9 39.6 1.0 HA3 I:GLY148 5.0 35.7 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