Manganese in PDB 7zz3: Cryo-Em Structure of "Bc React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa

Enzymatic activity of Cryo-Em Structure of "Bc React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa

Other elements in 7zz3:

Manganese Binding Sites:

Manganese binding site 1 out of 4 in 7zz3

Manganese Binding Sites List in 7zz3

Manganese binding site 1 out of 4 in the Cryo-Em Structure of "Bc React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Cryo-Em Structure of "Bc React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1203 b:92.1 occ:1.00 OD2 A:ASP534 2.1 73.0 1.0 OQ2 A:KCX703 2.1 80.1 1.0 NE2 A:HIS734 2.2 50.8 1.0 OQ1 A:KCX703 2.2 75.6 1.0 CE1 A:HIS732 2.4 58.8 1.0 CX A:KCX703 2.4 76.0 1.0 NE2 A:HIS732 2.5 54.4 1.0 CE1 A:HIS734 2.9 55.4 1.0 CG A:ASP534 3.0 58.5 1.0 OD1 A:ASP534 3.1 65.5 1.0 CD2 A:HIS734 3.4 58.2 1.0 NE2 A:GLN768 3.7 54.3 1.0 NZ A:KCX703 3.7 71.2 1.0 ND1 A:HIS732 3.7 62.7 1.0 CD2 A:HIS732 3.9 45.0 1.0 ND1 A:HIS734 4.1 59.8 1.0 O3 A:PYR1207 4.2 86.0 1.0 NH2 A:ARG533 4.3 50.4 1.0 CG A:HIS734 4.4 56.4 1.0 OE1 A:GLN768 4.4 59.1 1.0 CB A:ASP534 4.4 52.7 1.0 CD A:GLN768 4.4 56.2 1.0 CG A:HIS732 4.4 50.7 1.0 CE A:KCX703 4.6 67.7 1.0 CA A:MET705 5.0 69.8 1.0

Manganese binding site 2 out of 4 in 7zz3

Manganese Binding Sites List in 7zz3

Manganese binding site 2 out of 4 in the Cryo-Em Structure of "Bc React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Cryo-Em Structure of "Bc React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1202 b:57.3 occ:1.00 NE2 B:HIS734 2.3 36.5 1.0 OQ1 B:KCX703 2.4 54.5 1.0 OD2 B:ASP534 2.4 52.9 1.0 CE1 B:HIS732 2.4 49.1 1.0 NE2 B:HIS732 2.5 43.6 1.0 CE1 B:HIS734 2.9 32.7 1.0 CX B:KCX703 2.9 50.9 1.0 OQ2 B:KCX703 2.9 61.1 1.0 CG B:ASP534 3.2 37.2 1.0 OD1 B:ASP534 3.3 48.5 1.0 O B:HOH1338 3.5 61.8 1.0 CD2 B:HIS734 3.6 43.4 1.0 ND1 B:HIS732 3.7 50.7 1.0 NH2 B:ARG533 3.8 35.1 1.0 NE2 B:GLN768 3.8 36.4 1.0 CD2 B:HIS732 3.9 28.5 1.0 NZ B:KCX703 4.0 47.1 1.0 ND1 B:HIS734 4.1 44.2 1.0 CG B:HIS732 4.5 39.9 1.0 CG B:HIS734 4.5 42.0 1.0 CB B:ASP534 4.6 30.5 1.0 O3 B:PYR1206 4.6 58.9 1.0 CD B:GLN768 4.8 40.5 1.0 CA B:MET705 4.8 50.5 1.0 O B:MET705 4.9 55.8 1.0 OE1 B:GLN768 4.9 49.0 1.0

Manganese binding site 3 out of 4 in 7zz3

Manganese Binding Sites List in 7zz3

Manganese binding site 3 out of 4 in the Cryo-Em Structure of "Bc React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Cryo-Em Structure of "Bc React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn1202 b:78.7 occ:1.00 O C:HOH1328 2.2 60.9 1.0 NE2 C:HIS734 2.4 55.4 1.0 CE1 C:HIS732 2.4 66.4 1.0 OD2 C:ASP534 2.6 61.9 1.0 NE2 C:HIS732 2.9 62.9 1.0 CE1 C:HIS734 3.2 55.0 1.0 OQ1 C:KCX703 3.2 74.3 1.0 CG C:ASP534 3.4 52.0 1.0 OQ2 C:KCX703 3.4 78.5 1.0 OD1 C:ASP534 3.4 58.9 1.0 CD2 C:HIS734 3.5 59.6 1.0 CX C:KCX703 3.5 75.8 1.0 ND1 C:HIS732 3.6 66.4 1.0 O3 C:PYR1206 4.0 82.9 1.0 NE2 C:GLN768 4.1 51.1 1.0 CD2 C:HIS732 4.2 52.9 1.0 ND1 C:HIS734 4.4 60.0 1.0 NH2 C:ARG533 4.4 48.4 1.0 CG C:HIS734 4.5 60.8 1.0 CG C:HIS732 4.6 57.9 1.0 NZ C:KCX703 4.6 75.1 1.0 CB C:ASP534 4.8 44.1 1.0 O C:MET705 4.8 79.5 1.0

Manganese binding site 4 out of 4 in 7zz3

Manganese Binding Sites List in 7zz3

Manganese binding site 4 out of 4 in the Cryo-Em Structure of "Bc React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Cryo-Em Structure of "Bc React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn1202 b:77.7 occ:1.00 OQ2 D:KCX703 2.2 64.7 1.0 OD2 D:ASP534 2.2 62.3 1.0 OQ1 D:KCX703 2.2 64.2 1.0 NE2 D:HIS734 2.2 49.1 1.0 NE2 D:HIS732 2.3 50.2 1.0 CX D:KCX703 2.5 62.3 1.0 CE1 D:HIS734 3.0 46.8 1.0 CE1 D:HIS732 3.2 46.9 1.0 CG D:ASP534 3.2 53.1 1.0 CD2 D:HIS732 3.3 45.8 1.0 CD2 D:HIS734 3.4 47.0 1.0 OD1 D:ASP534 3.6 59.2 1.0 NE2 D:GLN768 3.8 51.2 1.0 NZ D:KCX703 3.8 60.6 1.0 ND1 D:HIS734 4.2 52.5 1.0 NH2 D:ARG533 4.3 52.4 1.0 ND1 D:HIS732 4.3 43.4 1.0 O3 D:PYR1206 4.4 77.4 1.0 CG D:HIS734 4.4 47.0 1.0 CG D:HIS732 4.4 44.7 1.0 CB D:ASP534 4.6 45.1 1.0 CD D:GLN768 4.7 49.5 1.0 OE1 D:GLN768 4.7 55.0 1.0 CE D:KCX703 4.8 55.1 1.0 CA D:MET705 4.9 53.3 1.0 O D:MET705 4.9 62.8 1.0 NH1 D:ARG533 5.0 45.7 1.0

Reference: