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Magnesium in PDB 8rn4: Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(T) Moiety (From "Influenza B Polymerase Pseudo-Symmetrical Dimer" | Local Refinement)

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

All present enzymatic activity of Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(T) 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(T) Moiety (From "Influenza B Polymerase Pseudo-Symmetrical Dimer" | Local Refinement) (pdb code 8rn4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(T) Moiety (From "Influenza B Polymerase Pseudo-Symmetrical Dimer" | Local Refinement), PDB code: 8rn4:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 8rn4

Go back to Magnesium Binding Sites List in 8rn4
Magnesium binding site 1 out of 2 in the Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(T) 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(T) Moiety (From "Influenza B Polymerase Pseudo-Symmetrical Dimer" | Local Refinement) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg801

b:18.0
occ:1.00
OD1 B:ASP444 1.9 37.6 1.0
H B:ASP444 2.5 35.7 1.0
HB3 B:SER443 2.6 34.9 1.0
H B:ASP445 2.7 36.1 1.0
HB2 B:ASP445 2.8 35.7 1.0
O B:SER442 2.8 39.5 1.0
CG B:ASP444 3.1 42.5 1.0
N B:ASP445 3.2 39.6 1.0
N B:ASP444 3.2 39.7 1.0
HG B:SER442 3.2 36.5 1.0
HB3 B:ASP445 3.3 35.8 1.0
CB B:ASP445 3.4 33.4 1.0
CB B:SER443 3.6 34.7 1.0
C B:ASP444 3.8 39.4 1.0
CA B:ASP444 3.8 33.5 1.0
CA B:ASP445 3.9 33.5 1.0
C B:SER442 3.9 34.3 1.0
OD2 B:ASP444 4.0 45.1 1.0
OG B:SER442 4.0 42.6 1.0
HG B:SER443 4.0 35.2 1.0
OG B:SER443 4.1 38.8 1.0
CB B:ASP444 4.1 35.1 1.0
C B:SER443 4.1 34.8 1.0
HB2 B:SER443 4.2 34.3 1.0
CA B:SER443 4.3 31.0 1.0
HA B:ASP445 4.5 35.4 1.0
HB3 B:ASP444 4.5 34.7 1.0
N B:SER443 4.6 35.5 1.0
CG B:ASP445 4.7 39.2 1.0
HA B:ASP444 4.8 33.6 1.0
HB2 B:ASP444 4.8 34.4 1.0
O B:ASP444 4.8 40.7 1.0
CB B:SER442 5.0 35.8 1.0
O B:ASP445 5.0 31.2 1.0

Magnesium binding site 2 out of 2 in 8rn4

Go back to Magnesium Binding Sites List in 8rn4
Magnesium binding site 2 out of 2 in the Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(T) 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 2 of Pseudo-Symmetrical Influenza B Polymerase Apo-Dimer, Endo(T) Moiety (From "Influenza B Polymerase Pseudo-Symmetrical Dimer" | Local Refinement) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg802

b:22.8
occ:1.00
OD1 B:ASP445 2.4 38.2 1.0
O B:GLY304 2.7 31.1 1.0
CG B:ASP445 3.3 39.2 1.0
OD2 B:ASP445 3.6 43.3 1.0
HB2 B:ASP305 3.7 27.2 1.0
OE2 B:GLU490 3.7 40.9 1.0
HG22 B:THR303 3.9 30.0 1.0
C B:GLY304 3.9 24.2 1.0
OE1 B:GLU490 3.9 45.5 1.0
HA B:PHE491 4.0 40.1 1.0
CD B:GLU490 4.1 42.7 1.0
HG23 B:THR303 4.1 31.1 1.0
HA B:ASP305 4.1 27.9 1.0
O B:GLU490 4.3 39.3 1.0
H B:THR492 4.3 46.9 1.0
O B:PHE446 4.4 26.9 1.0
CG2 B:THR303 4.4 31.0 1.0
H B:PHE446 4.5 31.1 1.0
CB B:ASP305 4.5 23.0 1.0
HA B:ASP445 4.5 35.4 1.0
H B:GLY304 4.5 26.5 1.0
CA B:ASP305 4.6 24.2 1.0
N B:GLY304 4.7 24.2 1.0
CB B:ASP445 4.7 33.4 1.0
N B:ASP305 4.7 23.1 1.0
HD1 B:PHE491 4.8 39.3 1.0
HB3 B:GLU490 4.8 38.2 1.0
HG21 B:THR303 4.9 29.9 1.0
C B:GLU490 4.9 39.5 1.0
CA B:PHE491 4.9 40.9 1.0
OD1 B:ASP305 4.9 37.8 1.0
CA B:GLY304 4.9 27.6 1.0
CG B:ASP305 5.0 30.6 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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