Atomistry » Zinc » PDB 6i0j-6iiu » 6i1d
Atomistry »
  Zinc »
    PDB 6i0j-6iiu »
      6i1d »

Zinc in PDB 6i1d: Structure of the YSH1-MPE1 Nuclease Complex From S.Cerevisiae

Protein crystallography data

The structure of Structure of the YSH1-MPE1 Nuclease Complex From S.Cerevisiae, PDB code: 6i1d was solved by C.H.Hill, V.Boreikaite, A.Kumar, A.Casanal, P.Kubik, G.Degliesposti, S.Maslen, A.Mariani, O.Von Loeffelholz, M.Girbig, M.Skehel, L.A.Passmore, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 62.14 / 2.28
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 43.380, 124.270, 63.450, 90.00, 103.21, 90.00
R / Rfree (%) 17.3 / 22.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the YSH1-MPE1 Nuclease Complex From S.Cerevisiae (pdb code 6i1d). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of the YSH1-MPE1 Nuclease Complex From S.Cerevisiae, PDB code: 6i1d:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6i1d

Go back to Zinc Binding Sites List in 6i1d
Zinc binding site 1 out of 2 in the Structure of the YSH1-MPE1 Nuclease Complex From S.Cerevisiae


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the YSH1-MPE1 Nuclease Complex From S.Cerevisiae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:55.7
occ:1.00
O A:HOH646 2.0 54.3 1.0
OD2 A:ASP184 2.1 51.5 1.0
NE2 A:HIS430 2.1 53.8 1.0
NE2 A:HIS73 2.3 42.2 1.0
OD2 A:ASP72 2.3 46.3 1.0
CD2 A:HIS73 3.0 36.0 1.0
CD2 A:HIS430 3.0 42.1 1.0
CE1 A:HIS430 3.0 43.3 1.0
CG A:ASP184 3.1 45.2 1.0
CG A:ASP72 3.3 54.6 1.0
OD1 A:ASP184 3.3 45.9 1.0
O A:HOH743 3.4 65.8 1.0
ZN A:ZN502 3.4 82.8 0.8
CE1 A:HIS73 3.5 45.1 1.0
OD1 A:ASP72 3.7 61.7 1.0
O A:HOH629 4.0 41.9 1.0
ND1 A:HIS430 4.1 43.9 1.0
CG A:HIS430 4.1 38.0 1.0
CG A:HIS73 4.3 43.7 1.0
NE2 A:HIS68 4.4 42.9 1.0
CB A:ASP184 4.4 43.3 1.0
ND1 A:HIS73 4.5 46.7 1.0
CE1 A:HIS408 4.5 49.0 1.0
CB A:ASP72 4.6 49.4 1.0
O A:HOH735 4.6 72.2 1.0
CE1 A:HIS68 4.6 42.1 1.0
CG1 A:VAL20 4.8 35.3 1.0
NE2 A:HIS408 4.9 51.7 1.0

Zinc binding site 2 out of 2 in 6i1d

Go back to Zinc Binding Sites List in 6i1d
Zinc binding site 2 out of 2 in the Structure of the YSH1-MPE1 Nuclease Complex From S.Cerevisiae


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the YSH1-MPE1 Nuclease Complex From S.Cerevisiae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:82.8
occ:0.82
NE2 A:HIS163 2.3 54.7 1.0
ND1 A:HIS70 2.4 54.1 1.0
O A:HOH646 2.4 54.3 1.0
OD2 A:ASP184 2.6 51.5 1.0
NE2 A:HIS68 2.6 42.9 1.0
CD2 A:HIS163 3.1 48.6 1.0
CE1 A:HIS163 3.2 50.5 1.0
CE1 A:HIS70 3.3 53.4 1.0
CD2 A:HIS68 3.4 39.5 1.0
ZN A:ZN501 3.4 55.7 1.0
O A:HOH735 3.4 72.2 1.0
CG A:HIS70 3.4 45.0 1.0
CG A:ASP184 3.5 45.2 1.0
CE1 A:HIS68 3.6 42.1 1.0
CB A:HIS70 3.7 40.4 1.0
CB A:ASP184 3.8 43.3 1.0
CD2 A:HIS73 4.2 36.0 1.0
CG A:HIS163 4.2 49.4 1.0
NE2 A:HIS73 4.3 42.2 1.0
ND1 A:HIS163 4.3 46.7 1.0
O A:HOH743 4.4 65.8 1.0
NE2 A:HIS70 4.5 54.8 1.0
CD2 A:HIS70 4.5 52.8 1.0
CG A:HIS68 4.6 46.0 1.0
NE2 A:HIS408 4.6 51.7 1.0
OD1 A:ASP72 4.6 61.7 1.0
CE1 A:HIS408 4.6 49.0 1.0
O A:HOH677 4.6 57.1 1.0
ND1 A:HIS68 4.7 49.2 1.0
OD1 A:ASP184 4.7 45.9 1.0
O A:HOH747 4.7 65.2 1.0
OD2 A:ASP72 4.8 46.3 1.0

Reference:

C.H.Hill, V.Boreikaite, A.Kumar, A.Casanal, P.Kubik, G.Degliesposti, S.Maslen, A.Mariani, O.Von Loeffelholz, M.Girbig, M.Skehel, L.A.Passmore. Activation of the Endonuclease That Defines Mrna 3' Ends Requires Incorporation Into An 8-Subunit Core Cleavage and Polyadenylation Factor Complex. Mol.Cell V. 73 1217 2019.
ISSN: ISSN 1097-2765
PubMed: 30737185
DOI: 10.1016/J.MOLCEL.2018.12.023
Page generated: Mon Oct 28 23:34:40 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