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Zinc in PDB 6lnd: Crystal Structure of Transposition Protein Tniq

Protein crystallography data

The structure of Crystal Structure of Transposition Protein Tniq, PDB code: 6lnd was solved by B.Wang, W.Xu, H.Yang, 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 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 66.277, 66.277, 178.584, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 22.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Transposition Protein Tniq (pdb code 6lnd). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Transposition Protein Tniq, PDB code: 6lnd:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6lnd

Go back to Zinc Binding Sites List in 6lnd
Zinc binding site 1 out of 2 in the Crystal Structure of Transposition Protein Tniq


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Transposition Protein Tniq within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Zn401

b:38.8
occ:1.00
SG K:CYS178 2.3 36.0 1.0
SG K:CYS163 2.3 41.0 1.0
SG K:CYS181 2.3 40.5 1.0
SG K:CYS161 2.5 37.7 1.0
CB K:CYS163 3.1 43.3 1.0
CB K:CYS161 3.1 36.0 1.0
CB K:CYS178 3.2 37.5 1.0
CB K:CYS181 3.3 42.5 1.0
N K:CYS181 3.8 40.1 1.0
N K:CYS163 4.1 42.2 1.0
CA K:CYS181 4.1 43.8 1.0
CA K:CYS163 4.1 43.7 1.0
O K:HOH580 4.5 32.6 1.0
CB K:LYS165 4.6 39.4 1.0
CA K:CYS161 4.6 35.7 1.0
CA K:CYS178 4.7 37.9 1.0
C K:CYS163 4.8 43.4 1.0
CB K:LYS180 4.8 42.9 1.0
C K:LYS180 4.9 41.9 1.0
C K:CYS181 4.9 41.0 1.0
N K:LYS165 4.9 43.0 1.0
C K:CYS161 4.9 37.9 1.0

Zinc binding site 2 out of 2 in 6lnd

Go back to Zinc Binding Sites List in 6lnd
Zinc binding site 2 out of 2 in the Crystal Structure of Transposition Protein Tniq


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Transposition Protein Tniq within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Zn402

b:30.2
occ:1.00
ND1 K:HIS153 2.1 28.6 1.0
SG K:CYS131 2.3 27.4 1.0
SG K:CYS128 2.3 29.1 1.0
SG K:CYS150 2.3 29.9 1.0
CE1 K:HIS153 2.9 28.3 1.0
CB K:CYS128 3.2 25.3 1.0
CG K:HIS153 3.2 29.5 1.0
CB K:CYS150 3.3 25.9 1.0
CB K:CYS131 3.4 25.3 1.0
N K:CYS131 3.5 28.6 1.0
CB K:HIS153 3.7 33.0 1.0
CA K:CYS131 3.9 27.4 1.0
NE2 K:HIS153 4.1 33.7 1.0
CD2 K:HIS153 4.3 31.5 1.0
N K:HIS153 4.3 38.2 1.0
CB K:LEU130 4.3 29.9 1.0
O K:HOH578 4.4 33.1 1.0
C K:LEU130 4.5 31.4 1.0
O K:HOH576 4.5 24.0 1.0
CA K:CYS128 4.6 26.8 1.0
CA K:HIS153 4.6 38.7 1.0
CA K:CYS150 4.7 29.6 1.0
CA K:LEU130 4.8 32.0 1.0
O K:CYS128 4.9 26.6 1.0
C K:CYS128 4.9 27.5 1.0
N K:LEU130 5.0 32.1 1.0
CB K:SER152 5.0 34.1 1.0

Reference:

B.Wang, W.Xu, H.Yang. Structural Basis of A TN7-Like Transposase Recruitment and Dna Loading to Crispr-Cas Surveillance Complex. Cell Res. V. 30 185 2020.
ISSN: ISSN 1001-0602
PubMed: 31913359
DOI: 10.1038/S41422-020-0274-0
Page generated: Tue Oct 29 02:42:02 2024

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