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Zinc in PDB 6v9q: Cryo-Em Structure of Cascade-Tniq Binary Complex

Zinc Binding Sites:

The binding sites of Zinc atom in the Cryo-Em Structure of Cascade-Tniq Binary Complex (pdb code 6v9q). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Cryo-Em Structure of Cascade-Tniq Binary Complex, PDB code: 6v9q:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 6v9q

Go back to Zinc Binding Sites List in 6v9q
Zinc binding site 1 out of 4 in the Cryo-Em Structure of Cascade-Tniq Binary Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of Cascade-Tniq Binary Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn401

b:0.2
occ:1.00
ND1 J:HIS153 2.2 0.7 1.0
SG J:CYS150 2.5 0.2 1.0
CB J:SER152 2.6 0.4 1.0
CE1 J:HIS153 2.8 0.7 1.0
CA J:SER152 3.1 0.4 1.0
C J:SER152 3.2 0.4 1.0
N J:HIS153 3.2 0.7 1.0
CG J:HIS153 3.3 0.7 1.0
N J:SER152 3.3 0.4 1.0
SG J:CYS131 3.5 0.5 1.0
OG J:SER152 3.6 0.4 1.0
O J:SER152 3.9 0.4 1.0
NE2 J:HIS153 3.9 0.7 1.0
CB J:HIS153 3.9 0.7 1.0
CA J:HIS153 4.1 0.7 1.0
CD2 J:HIS153 4.2 0.7 1.0
CB J:CYS150 4.3 0.2 1.0
C J:HIS151 4.6 0.2 1.0
N J:HIS151 4.8 0.2 1.0

Zinc binding site 2 out of 4 in 6v9q

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Zinc binding site 2 out of 4 in the Cryo-Em Structure of Cascade-Tniq Binary Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryo-Em Structure of Cascade-Tniq Binary Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn402

b:0.7
occ:1.00
SG J:CYS161 2.8 0.8 1.0
O J:PRO184 3.1 0.8 1.0
SG J:CYS181 3.2 0.8 1.0
O J:GLU183 3.5 0.5 1.0
CB J:GLU183 3.6 0.5 1.0
C J:PRO184 3.7 0.8 1.0
CA J:ILE185 3.8 0.8 1.0
C J:GLU183 3.8 0.5 1.0
N J:ILE185 4.0 0.8 1.0
CA J:GLU183 4.3 0.5 1.0
CG1 J:ILE185 4.4 0.8 1.0
N J:PRO184 4.5 0.8 1.0
N J:SER162 4.5 99.8 1.0
CB J:CYS161 4.6 0.8 1.0
CB J:CYS178 4.6 0.5 1.0
CB J:ILE185 4.6 0.8 1.0
CA J:PRO184 4.6 0.8 1.0
N J:THR186 4.7 0.3 1.0
CB J:SER162 4.7 99.8 1.0
N J:GLU183 4.7 0.5 1.0
C J:ILE185 4.8 0.8 1.0
CB J:CYS181 4.8 0.8 1.0
CG J:GLU183 4.8 0.5 1.0
OG J:SER162 4.8 99.8 1.0

Zinc binding site 3 out of 4 in 6v9q

Go back to Zinc Binding Sites List in 6v9q
Zinc binding site 3 out of 4 in the Cryo-Em Structure of Cascade-Tniq Binary Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cryo-Em Structure of Cascade-Tniq Binary Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Zn401

b:0.9
occ:1.00
SG I:CYS128 2.4 93.8 1.0
SG I:CYS150 2.5 95.0 1.0
SG I:CYS131 2.5 93.8 1.0
CB I:CYS128 2.7 93.8 1.0
CB I:CYS150 3.1 95.0 1.0
ND1 I:HIS153 3.7 96.2 1.0
CB I:CYS131 3.7 93.8 1.0
CA I:CYS128 4.2 93.8 1.0
CA I:CYS150 4.3 95.0 1.0
N I:CYS131 4.4 93.8 1.0
CZ2 I:TRP142 4.4 84.1 1.0
CE1 I:HIS153 4.4 96.2 1.0
CG I:HIS153 4.5 96.2 1.0
CB I:HIS153 4.6 96.2 1.0
CA I:CYS131 4.7 93.8 1.0
O I:CYS128 4.7 93.8 1.0
C I:CYS128 4.8 93.8 1.0
CG1 I:VAL155 4.9 92.0 1.0
NE1 I:TRP142 5.0 84.1 1.0

Zinc binding site 4 out of 4 in 6v9q

Go back to Zinc Binding Sites List in 6v9q
Zinc binding site 4 out of 4 in the Cryo-Em Structure of Cascade-Tniq Binary Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cryo-Em Structure of Cascade-Tniq Binary Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Zn402

b:0.7
occ:1.00
SG I:CYS178 2.5 94.5 1.0
SG I:CYS181 2.5 96.7 1.0
SG I:CYS161 2.6 97.9 1.0
CB I:CYS161 3.2 97.9 1.0
CB I:CYS178 3.3 94.5 1.0
CB I:CYS181 3.6 96.7 1.0
CB I:CYS163 3.6 97.3 1.0
N I:CYS181 3.9 96.7 1.0
SG I:CYS163 4.0 97.3 1.0
N I:CYS163 4.1 97.3 1.0
CA I:CYS181 4.4 96.7 1.0
CA I:CYS163 4.4 97.3 1.0
CA I:CYS161 4.6 97.9 1.0
N I:SER162 4.6 97.5 1.0
CB I:LYS180 4.8 95.8 1.0
CA I:CYS178 4.8 94.5 1.0
CB I:LYS165 4.8 94.8 1.0
N I:LYS180 4.9 95.8 1.0
C I:CYS161 4.9 97.9 1.0

Reference:

N.Jia, W.Xie, M.J.De La Cruz, E.T.Eng, D.J.Patel. Structure-Function Insights Into the Initial Step of Dna Integration By A Crispr-Cas-Transposon Complex. Cell Res. 2020.
ISSN: ISSN 1001-0602
PubMed: 31925391
DOI: 10.1038/S41422-019-0272-2
Page generated: Tue Oct 29 08:58:30 2024

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