Magnesium in PDB 8rn5: Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(R) Moiety (From "Influenza B Polymerase Pseudo-Symmetrical Dimer" | Local Refinement)

Enzymatic activity of Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(R) Moiety (From "Influenza B Polymerase Pseudo-Symmetrical Dimer" | Local Refinement)

All present enzymatic activity of Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(R) Moiety (From "Influenza B Polymerase Pseudo-Symmetrical Dimer" | Local Refinement):
2.7.7.48;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(R) Moiety (From "Influenza B Polymerase Pseudo-Symmetrical Dimer" | Local Refinement) (pdb code 8rn5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(R) Moiety (From "Influenza B Polymerase Pseudo-Symmetrical Dimer" | Local Refinement), PDB code: 8rn5:

Magnesium binding site 1 out of 1 in 8rn5

Go back to Magnesium Binding Sites List in 8rn5
Magnesium binding site 1 out of 1 in the Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(R) Moiety (From "Influenza B Polymerase Pseudo-Symmetrical Dimer" | Local Refinement)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(R) Moiety (From "Influenza B Polymerase Pseudo-Symmetrical Dimer" | Local Refinement) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg801

b:47.6
occ:1.00
OE2 B:GLU490 2.7 75.1 1.0
O B:GLY304 2.8 65.9 1.0
OD1 B:ASP445 2.9 75.2 1.0
HB2 B:ASP305 3.4 67.3 1.0
HG3 B:GLU490 3.5 70.6 1.0
CG B:ASP445 3.6 77.5 1.0
OD2 B:ASP445 3.6 77.7 1.0
HG23 B:THR303 3.7 63.3 1.0
HG22 B:THR303 3.8 62.3 1.0
CD B:GLU490 3.8 77.3 1.0
HA B:PHE491 3.8 66.1 1.0
C B:GLY304 3.9 62.6 1.0
O B:GLU490 4.1 74.6 1.0
CG B:GLU490 4.1 70.5 1.0
H B:THR492 4.1 69.8 1.0
HA B:ASP305 4.1 67.2 1.0
CG2 B:THR303 4.2 61.3 1.0
CB B:ASP305 4.3 66.1 1.0
HG2 B:GLU490 4.5 69.0 1.0
O B:PHE446 4.6 66.3 1.0
H B:GLY304 4.6 62.7 1.0
HG21 B:THR303 4.6 62.9 1.0
CA B:ASP305 4.6 61.1 1.0
H B:SER493 4.7 73.4 1.0
N B:GLY304 4.7 61.9 1.0
N B:ASP305 4.7 63.5 1.0
CA B:PHE491 4.7 63.5 1.0
C B:GLU490 4.7 68.2 1.0
HB3 B:ASP305 4.8 66.8 1.0
N B:THR492 4.8 72.5 1.0
H B:PHE446 4.8 60.9 1.0
HD1 B:PHE491 4.8 66.3 1.0
OE1 B:GLU490 4.9 77.7 1.0
HA B:ASP445 4.9 69.9 1.0
CA B:GLY304 4.9 64.3 1.0
CB B:ASP445 4.9 69.7 1.0
OD2 B:ASP305 5.0 73.4 1.0
N B:PHE491 5.0 64.5 1.0

Reference:

B.Arragain, T.Krischuns, M.Pelosse, P.Drncova, M.Blackledge, N.Naffakh, S.Cusack. Structures of Influenza A and B Replication Complexes Give Insight Into Avian to Human Host Adaptation and Reveal A Role of ANP32 As An Electrostatic Chaperone For the Apo-Polymerase. Nat Commun V. 15 6910 2024.
ISSN: ESSN 2041-1723
PubMed: 39160148
DOI: 10.1038/S41467-024-51007-3
Page generated: Fri Oct 4 17:43:17 2024

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