Atomistry » Magnesium » PDB 4mpo-4naa » 4n0n
Atomistry »
  Magnesium »
    PDB 4mpo-4naa »
      4n0n »

Magnesium in PDB 4n0n: Crystal Structure of Arterivirus Nonstructural Protein 10 (Helicase)

Enzymatic activity of Crystal Structure of Arterivirus Nonstructural Protein 10 (Helicase)

All present enzymatic activity of Crystal Structure of Arterivirus Nonstructural Protein 10 (Helicase):
2.7.7.48; 3.4.19.12; 3.6.4.12; 3.6.4.13;

Protein crystallography data

The structure of Crystal Structure of Arterivirus Nonstructural Protein 10 (Helicase), PDB code: 4n0n was solved by Z.Deng, Z.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 89.763, 91.041, 57.739, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 22.4

Other elements in 4n0n:

The structure of Crystal Structure of Arterivirus Nonstructural Protein 10 (Helicase) also contains other interesting chemical elements:

Zinc (Zn) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Arterivirus Nonstructural Protein 10 (Helicase) (pdb code 4n0n). 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 Arterivirus Nonstructural Protein 10 (Helicase), PDB code: 4n0n:

Magnesium binding site 1 out of 1 in 4n0n

Go back to Magnesium Binding Sites List in 4n0n
Magnesium binding site 1 out of 1 in the Crystal Structure of Arterivirus Nonstructural Protein 10 (Helicase)


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 Arterivirus Nonstructural Protein 10 (Helicase) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg509

b:52.4
occ:1.00
 OD2 A:ASP136 2.5 36.1 1.0
OG A:SER246 2.6 31.2 1.0
O A:HOH638 2.8 46.0 1.0
CG A:ASP136 3.2 36.4 1.0
NH2 A:ARG252 3.4 30.4 1.0
OD1 A:ASP136 3.4 36.2 1.0
CB A:SER246 3.5 31.9 1.0
OD2 A:ASP249 3.5 33.7 1.0
CG A:ASP249 3.6 32.0 1.0
OD1 A:ASP249 3.8 32.8 1.0
N A:ASP249 4.0 29.2 1.0
CB A:VAL248 4.0 30.7 1.0
NE2 A:HIS78 4.1 33.8 1.0
CB A:ASP249 4.3 29.5 1.0
CB A:ASP136 4.4 34.9 1.0
CD2 A:HIS78 4.5 34.0 1.0
O A:HOH602 4.5 35.0 1.0
CG2 A:VAL248 4.6 30.7 1.0
CA A:ASP249 4.6 29.5 1.0
C A:VAL248 4.7 29.1 1.0
O A:HOH668 4.7 47.1 1.0
CZ A:ARG252 4.7 30.4 1.0
CA A:VAL248 4.8 29.0 1.0
CG1 A:VAL248 4.8 30.5 1.0
O A:HOH691 4.9 51.5 1.0
CA A:SER246 4.9 30.5 1.0
N A:VAL248 4.9 29.9 1.0
OE1 A:GLN229 5.0 43.8 1.0

Reference:

Z.Deng, K.C.Lehmann, X.Li, C.Feng, G.Wang, Q.Zhang, X.Qi, L.Yu, X.Zhang, W.Feng, W.Wu, P.Gong, Y.Tao, C.C.Posthuma, E.J.Snijder, A.E.Gorbalenya, Z.Chen. Structural Basis For the Regulatory Function of A Complex Zinc-Binding Domain in A Replicative Arterivirus Helicase Resembling A Nonsense-Mediated Mrna Decay Helicase. Nucleic Acids Res. V. 42 3464 2014.
ISSN: ISSN 0305-1048
PubMed: 24369429
DOI: 10.1093/NAR/GKT1310
Page generated: Mon Aug 19 23:25:07 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy