Magnesium in PDB 7v1i: Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with An M7GMP-ARG28 Adduct and in Complex with Sah)

Enzymatic activity of Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with An M7GMP-ARG28 Adduct and in Complex with Sah)

All present enzymatic activity of Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with An M7GMP-ARG28 Adduct and in Complex with Sah):
3.4.21.91; 3.6.1.15; 3.6.4.13;

Protein crystallography data

The structure of Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with An M7GMP-ARG28 Adduct and in Complex with Sah), PDB code: 7v1i was solved by H.Jia, P.Gong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.73 / 2.06
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 35.232, 89.977, 45.686, 90, 91.25, 90
R / Rfree (%) 21.4 / 26.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with An M7GMP-ARG28 Adduct and in Complex with Sah) (pdb code 7v1i). 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 Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with An M7GMP-ARG28 Adduct and in Complex with Sah), PDB code: 7v1i:

Magnesium binding site 1 out of 1 in 7v1i

Go back to Magnesium Binding Sites List in 7v1i
Magnesium binding site 1 out of 1 in the Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with An M7GMP-ARG28 Adduct and in Complex with Sah)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with An M7GMP-ARG28 Adduct and in Complex with Sah) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg305

b:56.2
occ:1.00
 OP2 A:G7M302 2.0 48.0 0.2
O2A A:MGP303 2.0 46.1 0.4
O2A A:MGP303 2.0 46.2 0.4
O A:HOH438 2.9 51.3 1.0
O2B A:MGP303 3.2 57.2 0.4
P A:G7M302 3.3 47.6 0.2
O2C A:MGP303 3.3 56.5 0.4
PA A:MGP303 3.3 46.8 0.4
O2B A:MGP303 3.3 57.0 0.4
PA A:MGP303 3.4 46.6 0.4
OP1 A:G7M302 3.6 50.3 0.2
O3A A:MGP303 3.7 50.7 0.4
O3C A:MGP303 3.8 53.9 0.4
PB A:MGP303 3.9 56.0 0.4
O3A A:MGP303 4.0 51.4 0.4
O5' A:MGP303 4.0 40.5 0.4
O5' A:G7M302 4.0 41.5 0.2
PC A:MGP303 4.0 50.0 0.4
PB A:MGP303 4.1 55.7 0.4
O5' A:MGP303 4.1 41.0 0.4
CM7 A:MGP303 4.2 36.8 0.4
O3B A:MGP303 4.3 53.4 0.4
CN7 A:G7M302 4.3 37.0 0.2
O3B A:MGP303 4.4 53.8 0.4
CM7 A:MGP303 4.4 37.0 0.4
NH2 A:ARG28 4.4 49.5 0.2
O1A A:MGP303 4.4 47.2 0.4
O1A A:MGP303 4.4 47.2 0.4
NH1 A:ARG28 4.5 47.0 0.2
O A:HOH486 4.6 45.5 1.0
C8 A:MGP303 4.7 39.1 0.4
C8 A:G7M302 4.8 38.9 0.2
CZ A:ARG28 4.8 47.5 0.2
C8 A:MGP303 4.9 39.1 0.4
N7 A:MGP303 5.0 39.9 0.4

Reference:

H.Jia, Y.Zhong, C.Peng, P.Gong. Crystal Structures of Flavivirus NS5 Guanylyltransferase Reveal A Gmp-Arginine Adduct. J.Virol. V. 96 41822 2022.
ISSN: ESSN 1098-5514
PubMed: 35758665
DOI: 10.1128/JVI.00418-22
Page generated: Fri Apr 7 00:15:56 2023

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