Magnesium in PDB 8rmp: Influenza Polymerase A/H7N9-4M (Endo(R) | CORE1)

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Influenza Polymerase A/H7N9-4M (Endo(R) | CORE1) (pdb code 8rmp). 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 Influenza Polymerase A/H7N9-4M (Endo(R) | CORE1), PDB code: 8rmp:

Magnesium binding site 1 out of 1 in 8rmp

Go back to Magnesium Binding Sites List in 8rmp
Magnesium binding site 1 out of 1 in the Influenza Polymerase A/H7N9-4M (Endo(R) | CORE1)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Influenza Polymerase A/H7N9-4M (Endo(R) | CORE1) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg801

b:67.3
occ:1.00
OD2 B:ASP446 1.9 86.3 1.0
CG B:ASP446 3.0 89.5 1.0
HG23 B:THR303 3.2 64.8 1.0
HG22 B:THR303 3.3 65.3 1.0
OE1 B:GLU491 3.3 77.3 1.0
O B:GLY304 3.6 73.2 1.0
OD1 B:ASP446 3.6 90.8 1.0
CG2 B:THR303 3.7 67.1 1.0
H B:THR493 3.8 80.2 1.0
HA B:PHE492 3.8 73.8 1.0
H B:GLY304 4.0 67.3 1.0
CD B:GLU491 4.0 76.0 1.0
HB3 B:ASP446 4.0 80.5 1.0
HG21 B:THR303 4.1 63.6 1.0
C B:GLY304 4.1 69.9 1.0
H B:PHE447 4.1 66.2 1.0
OE2 B:GLU491 4.1 66.3 1.0
CB B:ASP446 4.1 81.0 1.0
N B:GLY304 4.2 63.6 1.0
O B:GLU491 4.3 71.6 1.0
OD1 B:ASP305 4.3 81.3 1.0
CG B:ASP305 4.4 86.6 1.0
HA B:ASP446 4.4 81.7 1.0
OD2 B:ASP305 4.4 87.2 1.0
O B:PHE447 4.4 69.8 1.0
N B:THR493 4.6 80.6 1.0
N B:ASP305 4.6 70.5 1.0
HA B:ASP305 4.6 74.8 1.0
CA B:PHE492 4.7 66.8 1.0
C B:THR303 4.7 65.1 1.0
CA B:GLY304 4.7 68.2 1.0
C B:GLU491 4.8 70.0 1.0
N B:PHE447 4.8 62.5 1.0
CA B:ASP446 4.8 83.1 1.0
HB3 B:GLU491 4.8 71.5 1.0
HB2 B:ASP446 4.9 80.6 1.0
HA B:THR303 4.9 64.2 1.0
HZ1 A:LYS664 4.9 54.5 1.0
HB2 B:ASP305 4.9 75.9 1.0
CA B:ASP305 5.0 72.6 1.0
N B:PHE492 5.0 71.3 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 17:41:07 2024

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