Magnesium in PDB 7e51: Structure of Pep Bound Enolase From Mycobacterium Tuberculosis

All present enzymatic activity of Structure of Pep Bound Enolase From Mycobacterium Tuberculosis:
4.2.1.11;

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Magnesium atom in the Structure of Pep Bound Enolase From Mycobacterium Tuberculosis (pdb code 7e51). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 16 binding sites of Magnesium where determined in the Structure of Pep Bound Enolase From Mycobacterium Tuberculosis, PDB code: 7e51:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 16 in the Structure of Pep Bound Enolase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Pep Bound Enolase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:56.8 occ:1.00 OG A:SER42 2.3 65.5 1.0 O2P A:PEP501 2.4 57.0 1.0 O2' A:PEP501 3.4 57.0 1.0 P A:PEP501 3.4 57.0 1.0 NZ A:LYS335 3.5 47.5 1.0 OD2 A:ASP310 3.5 69.8 1.0 CB A:SER42 3.5 65.5 1.0 O3P A:PEP501 3.5 57.0 1.0 O A:SER42 3.6 65.5 1.0 O2 A:PEP501 4.1 57.0 1.0 OD1 A:ASP311 4.2 75.5 1.0 MG A:MG503 4.2 66.5 1.0 OD2 A:ASP311 4.2 75.5 1.0 OD1 A:ASP310 4.3 69.8 1.0 CG A:ASP310 4.3 69.8 1.0 C1 A:PEP501 4.3 57.0 1.0 C2 A:PEP501 4.4 57.0 1.0 C A:SER42 4.5 65.5 1.0 CA A:SER42 4.6 65.5 1.0 CG A:ASP311 4.6 75.5 1.0 O1P A:PEP501 4.7 57.0 1.0 NH2 A:ARG364 4.9 45.6 1.0 CE A:LYS335 5.0 47.5 1.0

Magnesium binding site 2 out of 16 in the Structure of Pep Bound Enolase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Pep Bound Enolase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg503 b:66.5 occ:1.00 OD2 A:ASP310 2.1 69.8 1.0 OE2 A:GLU283 2.5 70.2 1.0 O2' A:PEP501 2.6 57.0 1.0 OD2 A:ASP241 2.9 75.3 1.0 OD1 A:ASP241 3.0 75.3 1.0 CG A:ASP310 3.2 69.8 1.0 CG A:ASP241 3.3 75.3 1.0 CD A:GLU283 3.5 70.2 1.0 C1 A:PEP501 3.6 57.0 1.0 CB A:ASP310 3.8 69.8 1.0 O1 A:PEP501 4.0 57.0 1.0 OD1 A:ASP310 4.2 69.8 1.0 MG A:MG502 4.2 56.8 1.0 OE1 A:GLU283 4.2 70.2 1.0 OE1 A:GLN162 4.3 82.7 1.0 CG A:GLU283 4.4 70.2 1.0 NZ A:LYS335 4.6 47.5 1.0 CD1 A:LEU333 4.6 48.5 1.0 CB A:ASP241 4.7 75.3 1.0 NZ A:LYS386 4.8 41.7 1.0 C2 A:PEP501 4.9 57.0 1.0 OD2 A:ASP284 5.0 77.9 1.0

Magnesium binding site 3 out of 16 in the Structure of Pep Bound Enolase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Pep Bound Enolase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:73.1 occ:1.00 OG B:SER42 2.5 71.0 1.0 O B:SER42 2.6 71.0 1.0 O2P B:PEP501 2.9 59.1 1.0 C B:SER42 3.5 71.0 1.0 CB B:SER42 3.6 71.0 1.0 CA B:SER42 3.8 71.0 1.0 N B:SER42 4.0 71.0 1.0 P B:PEP501 4.0 59.1 1.0 O1P B:PEP501 4.0 59.1 1.0 N B:THR43 4.5 79.0 1.0 O3P B:PEP501 4.7 59.1 1.0 O B:THR43 4.8 79.0 1.0 OE2 B:GLU246 4.9 102.7 1.0 NH2 B:ARG364 4.9 46.4 1.0

Magnesium binding site 4 out of 16 in the Structure of Pep Bound Enolase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of Pep Bound Enolase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg503 b:68.7 occ:1.00 OE2 B:GLU283 2.1 72.9 1.0 O1 B:PEP501 2.3 59.1 1.0 OD2 B:ASP310 2.7 71.1 1.0 OD2 B:ASP241 3.0 76.1 1.0 CD B:GLU283 3.3 72.9 1.0 OD1 B:ASP241 3.4 76.1 1.0 C1 B:PEP501 3.4 59.1 1.0 CG B:ASP241 3.6 76.1 1.0 O2' B:PEP501 3.8 59.1 1.0 CG B:ASP310 3.9 71.1 1.0 OD2 B:ASP284 3.9 80.8 1.0 NE2 B:GLN162 4.1 83.1 1.0 OE1 B:GLU283 4.1 72.9 1.0 CG B:GLU283 4.2 72.9 1.0 NZ B:LYS335 4.2 47.7 1.0 CB B:ASP310 4.6 71.1 1.0 C2 B:PEP501 4.6 59.1 1.0 CD1 B:LEU333 4.7 49.2 1.0 O2P B:PEP501 4.8 59.1 1.0 OD1 B:ASP310 4.8 71.1 1.0 CB B:ALA243 4.9 87.3 1.0 OD2 B:ASP311 5.0 77.8 1.0

Magnesium binding site 5 out of 16 in the Structure of Pep Bound Enolase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Structure of Pep Bound Enolase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg502 b:63.2 occ:1.00 O2P C:PEP501 2.1 57.4 1.0 O C:SER42 2.7 67.3 1.0 OG C:SER42 3.2 67.3 1.0 P C:PEP501 3.4 57.4 1.0 O3P C:PEP501 3.6 57.4 1.0 C C:SER42 3.8 67.3 1.0 O1P C:PEP501 4.3 57.4 1.0 CB C:SER42 4.3 67.3 1.0 O2' C:PEP501 4.3 57.4 1.0 NZ C:LYS335 4.4 46.4 1.0 OD1 C:ASP311 4.4 74.5 1.0 CA C:SER42 4.4 67.3 1.0 O2 C:PEP501 4.5 57.4 1.0 N C:SER42 4.5 67.3 1.0 NH2 C:ARG364 4.6 43.9 1.0 OD2 C:ASP310 4.8 69.2 1.0 N C:THR43 4.9 76.4 1.0 OD2 C:ASP311 5.0 74.5 1.0

Magnesium binding site 6 out of 16 in the Structure of Pep Bound Enolase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Structure of Pep Bound Enolase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg503 b:63.4 occ:1.00 OE2 C:GLU283 2.1 71.0 1.0 OD2 C:ASP310 2.1 69.2 1.0 O2' C:PEP501 2.5 57.4 1.0 OD2 C:ASP241 2.8 74.3 1.0 OD1 C:ASP241 3.0 74.3 1.0 CG C:ASP241 3.2 74.3 1.0 CG C:ASP310 3.2 69.2 1.0 CD C:GLU283 3.3 71.0 1.0 C1 C:PEP501 3.4 57.4 1.0 O1 C:PEP501 3.7 57.4 1.0 CB C:ASP310 3.8 69.2 1.0 OE1 C:GLU283 4.1 71.0 1.0 CG C:GLU283 4.1 71.0 1.0 NE2 C:GLN162 4.2 84.4 1.0 OD1 C:ASP310 4.2 69.2 1.0 NZ C:LYS386 4.2 42.9 1.0 NZ C:LYS335 4.4 46.4 1.0 CB C:ASP241 4.7 74.3 1.0 C2 C:PEP501 4.8 57.4 1.0 CD2 C:LEU333 4.9 47.5 1.0 CB C:ALA243 4.9 88.5 1.0 OD2 C:ASP284 5.0 77.6 1.0

Magnesium binding site 7 out of 16 in the Structure of Pep Bound Enolase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Structure of Pep Bound Enolase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg502 b:59.8 occ:1.00 O2P D:PEP501 2.1 57.0 1.0 OG D:SER42 2.7 66.3 1.0 P D:PEP501 3.4 57.0 1.0 O1P D:PEP501 3.8 57.0 1.0 O1 D:PEP501 3.8 57.0 1.0 CB D:SER42 3.9 66.3 1.0 NZ D:LYS335 4.0 47.1 1.0 OD1 D:ASP311 4.1 76.9 1.0 OD2 D:ASP310 4.3 70.5 1.0 O2 D:PEP501 4.3 57.0 1.0 O3P D:PEP501 4.4 57.0 1.0 N D:SER42 4.6 66.3 1.0 OD2 D:ASP311 4.7 76.9 1.0 NH2 D:ARG364 4.7 45.7 1.0 C1 D:PEP501 4.7 57.0 1.0 C2 D:PEP501 4.8 57.0 1.0 O D:SER42 4.8 66.3 1.0 CA D:SER42 4.8 66.3 1.0 CG D:ASP311 4.9 76.9 1.0 MG D:MG503 4.9 64.5 1.0

Magnesium binding site 8 out of 16 in the Structure of Pep Bound Enolase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Structure of Pep Bound Enolase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg503 b:64.5 occ:1.00 OD2 D:ASP310 2.1 70.5 1.0 OE2 D:GLU283 2.1 70.3 1.0 O1 D:PEP501 2.5 57.0 1.0 OD2 D:ASP241 2.7 72.8 1.0 OD1 D:ASP241 3.0 72.8 1.0 CG D:ASP241 3.2 72.8 1.0 CG D:ASP310 3.2 70.5 1.0 CD D:GLU283 3.3 70.3 1.0 C1 D:PEP501 3.5 57.0 1.0 O2' D:PEP501 3.7 57.0 1.0 CB D:ASP310 3.8 70.5 1.0 NE2 D:GLN162 3.9 81.6 1.0 OE1 D:GLU283 4.1 70.3 1.0 CG D:GLU283 4.1 70.3 1.0 OD1 D:ASP310 4.2 70.5 1.0 NZ D:LYS386 4.2 43.4 1.0 NZ D:LYS335 4.4 47.1 1.0 CB D:ASP241 4.7 72.8 1.0 C2 D:PEP501 4.8 57.0 1.0 CB D:ALA243 4.8 87.7 1.0 MG D:MG502 4.9 59.8 1.0 CD2 D:LEU333 4.9 49.1 1.0 OD2 D:ASP284 4.9 78.2 1.0

Magnesium binding site 9 out of 16 in the Structure of Pep Bound Enolase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Structure of Pep Bound Enolase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg502 b:59.2 occ:1.00 O2P E:PEP501 2.1 58.9 1.0 OG E:SER42 2.1 66.7 1.0 CB E:SER42 3.4 66.7 1.0 P E:PEP501 3.5 58.9 1.0 O2' E:PEP501 3.6 58.9 1.0 NZ E:LYS335 3.9 48.0 1.0 O3P E:PEP501 3.9 58.9 1.0 O E:SER42 4.0 66.7 1.0 OD2 E:ASP310 4.1 70.4 1.0 OD1 E:ASP311 4.1 75.5 1.0 O2 E:PEP501 4.3 58.9 1.0 CA E:SER42 4.4 66.7 1.0 O1P E:PEP501 4.5 58.9 1.0 C1 E:PEP501 4.5 58.9 1.0 C E:SER42 4.6 66.7 1.0 OD2 E:ASP311 4.6 75.5 1.0 MG E:MG503 4.6 66.2 1.0 C2 E:PEP501 4.7 58.9 1.0 N E:SER42 4.7 66.7 1.0 CG E:ASP311 4.8 75.5 1.0 NH2 E:ARG364 4.8 45.9 1.0 CG E:ASP310 4.9 70.4 1.0 OD1 E:ASP310 4.9 70.4 1.0

Magnesium binding site 10 out of 16 in the Structure of Pep Bound Enolase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Structure of Pep Bound Enolase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg503 b:66.2 occ:1.00 OE2 E:GLU283 2.1 70.2 1.0 OD2 E:ASP310 2.1 70.4 1.0 O2' E:PEP501 2.5 58.9 1.0 OD2 E:ASP241 2.7 74.7 1.0 OD1 E:ASP241 3.0 74.7 1.0 CG E:ASP241 3.2 74.7 1.0 CG E:ASP310 3.2 70.4 1.0 CD E:GLU283 3.3 70.2 1.0 C1 E:PEP501 3.4 58.9 1.0 O1 E:PEP501 3.6 58.9 1.0 CB E:ASP310 3.9 70.4 1.0 NE2 E:GLN162 4.0 82.6 1.0 OE1 E:GLU283 4.1 70.2 1.0 CG E:GLU283 4.1 70.2 1.0 NZ E:LYS386 4.2 43.5 1.0 OD1 E:ASP310 4.2 70.4 1.0 NZ E:LYS335 4.4 48.0 1.0 MG E:MG502 4.6 59.2 1.0 CB E:ASP241 4.7 74.7 1.0 C2 E:PEP501 4.8 58.9 1.0 CB E:ALA243 4.9 88.2 1.0 CD2 E:LEU333 4.9 49.5 1.0 OD2 E:ASP284 5.0 78.0 1.0

M.Ahmad, B.Jha, S.Bose, R.Mariadasee, A.Dwivedy, S.Tiwari, R.Pal, D.Kar, T.Parish, J.Jeyakanthan, K.R.Vinothkumar, B.K.Biswal. Structural Snapshots of Mycobacterium Tuberculosis Enolase Reveal Dual Mode of 2PG Binding and Its Implication in Enzyme Catalysis. To Be Published.