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Manganese in PDB 5fj7: Structure of the P2 Polymerase Inside in Vitro Assembled Bacteriophage PHI6 Polymerase Complex, with P1 Included

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of the P2 Polymerase Inside in Vitro Assembled Bacteriophage PHI6 Polymerase Complex, with P1 Included (pdb code 5fj7). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Structure of the P2 Polymerase Inside in Vitro Assembled Bacteriophage PHI6 Polymerase Complex, with P1 Included, PDB code: 5fj7:

Manganese binding site 1 out of 1 in 5fj7

Go back to Manganese Binding Sites List in 5fj7
Manganese binding site 1 out of 1 in the Structure of the P2 Polymerase Inside in Vitro Assembled Bacteriophage PHI6 Polymerase Complex, with P1 Included


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of the P2 Polymerase Inside in Vitro Assembled Bacteriophage PHI6 Polymerase Complex, with P1 Included within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn1665

b:0.4
occ:1.00
N C:GLY498 1.8 0.5 1.0
N C:LEU497 1.9 0.1 1.0
C C:PHE496 1.9 0.3 1.0
N C:PHE496 2.5 0.1 1.0
CA C:PHE496 2.5 0.8 1.0
C C:LEU497 2.5 0.1 1.0
O C:PHE496 2.6 0.8 1.0
CA C:LEU497 2.6 0.5 1.0
CA C:GLY498 2.9 0.3 1.0
N C:ASP499 3.0 0.5 1.0
C C:ALA495 3.1 0.8 1.0
C C:GLY498 3.4 0.7 1.0
OD2 C:ASP454 3.5 0.6 1.0
CB C:ALA495 3.5 0.1 1.0
O C:ALA495 3.6 0.6 1.0
O C:LEU497 3.7 0.2 1.0
CB C:LEU497 3.9 1.0 1.0
CA C:ALA495 3.9 0.2 1.0
CB C:PHE496 3.9 1.0 1.0
CA C:ASP499 4.1 0.1 1.0
O C:ASP499 4.2 0.1 1.0
C C:ASP499 4.3 0.0 1.0
CG C:ASP454 4.5 0.8 1.0
O C:GLY498 4.6 1.0 1.0
CB C:ASP499 4.6 0.6 1.0
OD1 C:ASP454 4.7 0.7 1.0
CG C:PHE496 4.7 0.3 1.0

Reference:

S.L.Ilca, A.Kotecha, X.Sun, M.M.Poranen, D.I.Stuart, J.T.Huiskonen. Localized Reconstruction of Subunits From Electron Cryomicroscopy Images of Macromolecular Complexes. Nat.Commun. V. 6 8843 2015.
ISSN: ESSN 2041-1723
PubMed: 26534841
DOI: 10.1038/NCOMMS9843
Page generated: Sun Oct 6 00:14:24 2024

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