Magnesium in PDB 8xy6: Asfv Rnap M1249L C-Tail Occupied COMPLEX3 (MCOC3)

Enzymatic activity of Asfv Rnap M1249L C-Tail Occupied COMPLEX3 (MCOC3)

All present enzymatic activity of Asfv Rnap M1249L C-Tail Occupied COMPLEX3 (MCOC3):
2.7.7.6;

Other elements in 8xy6:

The structure of Asfv Rnap M1249L C-Tail Occupied COMPLEX3 (MCOC3) also contains other interesting chemical elements:

Zinc (Zn) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Asfv Rnap M1249L C-Tail Occupied COMPLEX3 (MCOC3) (pdb code 8xy6). 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 Asfv Rnap M1249L C-Tail Occupied COMPLEX3 (MCOC3), PDB code: 8xy6:

Magnesium binding site 1 out of 1 in 8xy6

Go back to Magnesium Binding Sites List in 8xy6
Magnesium binding site 1 out of 1 in the Asfv Rnap M1249L C-Tail Occupied COMPLEX3 (MCOC3)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Asfv Rnap M1249L C-Tail Occupied COMPLEX3 (MCOC3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1503

b:53.3
occ:1.00
OD1 A:ASP459 2.0 67.4 1.0
OD1 A:ASP461 2.0 51.9 1.0
OD1 A:ASP457 2.2 59.7 1.0
CG A:ASP459 2.6 58.0 1.0
OD2 A:ASP459 2.7 57.6 1.0
CG A:ASP461 2.8 53.7 1.0
OD2 A:ASP461 3.1 58.5 1.0
CG A:ASP457 3.2 57.5 1.0
OD2 A:ASP457 3.5 61.6 1.0
O I:ALA1247 4.0 88.2 1.0
CB A:ASP459 4.1 47.8 1.0
O I:ASN1245 4.2 85.8 1.0
CB A:ASP461 4.2 50.8 1.0
O A:ASP457 4.4 54.9 1.0
N A:ASP461 4.5 52.0 1.0
CB A:ASP457 4.5 46.6 1.0
N A:ASP459 4.5 58.8 1.0
N A:ASP457 4.6 52.0 1.0
CA A:ASP461 4.7 53.1 1.0
C A:ASP457 4.7 46.2 1.0
CA A:ASP459 4.7 44.4 1.0
O I:ASP1244 4.7 91.3 1.0
C A:ASP459 4.8 54.5 1.0
N A:GLY460 4.8 49.2 1.0
CA A:ASP457 4.8 46.0 1.0
C I:ASN1245 5.0 82.9 1.0

Reference:

G.Zhu, F.Xi, W.Zeng, Y.Zhao, W.Cao, C.Liu, F.Yang, Y.Ru, S.Xiao, S.Zhang, H.Liu, H.Tian, F.Yang, B.Lu, S.Sun, H.Song, B.Sun, X.Zhao, L.Tang, K.Li, J.He, J.Guo, Y.Zhu, Z.Zhu, F.Sun, H.Zheng. Structural Basis of Rna Polymerase Complexes in African Swine Fever Virus. Nat Commun V. 16 501 2025.
ISSN: ESSN 2041-1723
PubMed: 39779680
DOI: 10.1038/S41467-024-55683-Z
Page generated: Sat Feb 8 20:52:01 2025

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