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Manganese in PDB 3wro: Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication

Protein crystallography data

The structure of Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication, PDB code: 3wro was solved by S.K.Tewary, H.Zhao, L.Tang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.50 / 1.48
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 57.240, 121.350, 41.750, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 19.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication (pdb code 3wro). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication, PDB code: 3wro:

Manganese binding site 1 out of 1 in 3wro

Go back to Manganese Binding Sites List in 3wro
Manganese binding site 1 out of 1 in the Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn301

b:15.5
occ:0.78
OE1 A:GLU119 2.1 19.3 1.0
O A:HOH434 2.2 22.0 1.0
O A:HOH527 2.2 24.1 1.0
NE2 A:HIS129 2.2 17.9 1.0
O A:HOH529 2.3 22.0 1.0
NE2 A:HIS127 2.3 19.4 1.0
CE1 A:HIS129 3.2 18.7 1.0
CD2 A:HIS129 3.2 17.6 1.0
CE1 A:HIS127 3.3 19.2 1.0
CD2 A:HIS127 3.3 18.4 1.0
CD A:GLU119 3.3 14.5 0.7
CB A:GLU119 4.1 16.9 1.0
O A:HOH457 4.1 29.5 1.0
OE2 A:GLU119 4.2 18.6 1.0
CG A:GLU119 4.2 17.0 1.0
NZ A:LYS214 4.2 23.1 1.0
ND1 A:HIS129 4.3 16.5 1.0
CG A:HIS129 4.4 15.5 1.0
ND1 A:HIS127 4.4 15.1 1.0
CG A:HIS127 4.4 14.7 1.0
O A:HOH570 4.6 32.0 1.0

Reference:

S.K.Tewary, L.Liang, Z.Lin, A.Lynn, S.F.Cotmore, P.Tattersall, H.Zhao, L.Tang. Structures of Minute Virus of Mice Replication Initiator Protein N-Terminal Domain: Insights Into Dna Nicking and Origin Binding. Virology V.476C 61 2014.
ISSN: ISSN 0042-6822
PubMed: 25528417
DOI: 10.1016/J.VIROL.2014.11.022
Page generated: Tue Dec 15 04:17:08 2020

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