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Magnesium in PDB 8xxt: Asfv Rnap M1249L C-Tail Occupied COMPLEX2 (MCOC2)

Enzymatic activity of Asfv Rnap M1249L C-Tail Occupied COMPLEX2 (MCOC2)

All present enzymatic activity of Asfv Rnap M1249L C-Tail Occupied COMPLEX2 (MCOC2):
2.7.7.6;

Other elements in 8xxt:

The structure of Asfv Rnap M1249L C-Tail Occupied COMPLEX2 (MCOC2) also contains other interesting chemical elements:

Zinc (Zn) 7 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Asfv Rnap M1249L C-Tail Occupied COMPLEX2 (MCOC2) (pdb code 8xxt). 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 COMPLEX2 (MCOC2), PDB code: 8xxt:

Magnesium binding site 1 out of 1 in 8xxt

Go back to Magnesium Binding Sites List in 8xxt
Magnesium binding site 1 out of 1 in the Asfv Rnap M1249L C-Tail Occupied COMPLEX2 (MCOC2)


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 COMPLEX2 (MCOC2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1503

b:67.3
occ:1.00
OD1 A:ASP459 2.0 79.4 1.0
OD1 A:ASP461 2.1 66.0 1.0
OD1 A:ASP457 2.1 69.1 1.0
CG A:ASP459 2.6 70.4 1.0
OD2 A:ASP459 2.7 74.1 1.0
CG A:ASP461 2.8 69.8 1.0
OD2 A:ASP461 2.9 79.8 1.0
CG A:ASP457 3.0 69.1 1.0
OD2 A:ASP457 3.3 77.7 1.0
CB A:ASP459 4.1 61.6 1.0
CB A:ASP461 4.2 56.3 1.0
O A:ASP457 4.3 67.1 1.0
O I:ALA1247 4.3 101.0 1.0
CB A:ASP457 4.4 53.8 1.0
N A:ASP457 4.5 65.9 1.0
N A:ASP459 4.5 63.4 1.0
O I:ASP1244 4.5 86.8 1.0
N A:ASP461 4.5 60.2 1.0
C A:ASP457 4.6 64.5 1.0
O I:ASN1245 4.6 87.4 1.0
CA A:ASP459 4.7 51.9 1.0
CA A:ASP457 4.7 58.6 1.0
CA A:ASP461 4.7 60.8 1.0
C A:ASP459 4.8 55.7 1.0
CA I:ASN1245 4.9 81.0 1.0
N A:GLY460 4.9 59.2 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: Fri Aug 15 21:14:41 2025

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