Zinc in PDB 7tw7: Structure of NSP14 N7-Methyltransferase Domain Fused with Telsam Bound to Sam

Protein crystallography data

The structure of Structure of NSP14 N7-Methyltransferase Domain Fused with Telsam Bound to Sam, PDB code: 7tw7 was solved by J.Kottur, A.K.Aggarwal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.21 / 1.62
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 108.774, 108.774, 48.527, 90, 90, 120
R / Rfree (%) 17.9 / 21.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of NSP14 N7-Methyltransferase Domain Fused with Telsam Bound to Sam (pdb code 7tw7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of NSP14 N7-Methyltransferase Domain Fused with Telsam Bound to Sam, PDB code: 7tw7:

Zinc binding site 1 out of 1 in 7tw7

Go back to Zinc Binding Sites List in 7tw7
Zinc binding site 1 out of 1 in the Structure of NSP14 N7-Methyltransferase Domain Fused with Telsam Bound to Sam


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of NSP14 N7-Methyltransferase Domain Fused with Telsam Bound to Sam within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:13.5
occ:1.00
ND1 A:HIS487 2.1 11.5 1.0
SG A:CYS477 2.3 13.2 1.0
SG A:CYS484 2.3 14.7 1.0
SG A:CYS452 2.3 14.5 1.0
HB3 A:CYS477 2.9 21.7 1.0
CE1 A:HIS487 3.0 12.5 1.0
HB3 A:CYS452 3.1 16.1 1.0
HE1 A:HIS487 3.1 15.2 1.0
HB2 A:HIS487 3.1 14.4 1.0
HA A:CYS452 3.1 21.9 1.0
CB A:CYS452 3.2 13.2 1.0
H A:CYS484 3.2 19.4 1.0
HB3 A:CYS484 3.2 19.0 1.0
CB A:CYS477 3.2 17.9 1.0
CG A:HIS487 3.2 12.5 1.0
CB A:CYS484 3.4 15.7 1.0
H A:CYS477 3.6 12.6 1.0
CA A:CYS452 3.6 18.1 1.0
CB A:HIS487 3.7 11.9 1.0
HB2 A:CYS477 3.8 21.7 1.0
HB A:THR475 3.8 17.5 1.0
N A:CYS484 4.0 16.0 1.0
H A:HIS487 4.0 20.9 1.0
HB2 A:CYS452 4.0 16.1 1.0
HB2 A:CYS484 4.1 19.0 1.0
NE2 A:HIS487 4.2 11.0 1.0
HB3 A:HIS487 4.2 14.4 1.0
HG1 A:THR475 4.2 15.8 1.0
CA A:CYS484 4.3 18.2 1.0
CD2 A:HIS487 4.3 16.0 1.0
N A:CYS477 4.3 10.3 1.0
H A:GLU453 4.3 26.3 1.0
CA A:CYS477 4.4 14.1 1.0
HG13 A:VAL483 4.5 19.0 1.0
N A:CYS452 4.5 16.6 1.0
CB A:THR475 4.6 14.4 1.0
OG1 A:THR475 4.6 13.0 1.0
HD2 A:HIS486 4.7 37.1 1.0
N A:HIS487 4.7 17.2 1.0
H A:CYS452 4.7 20.1 1.0
HA A:VAL483 4.7 29.6 1.0
C A:CYS452 4.8 18.3 1.0
CA A:HIS487 4.8 14.0 1.0
HG21 A:THR475 4.8 21.3 1.0
N A:GLU453 4.9 21.8 1.0
HB3 A:HIS486 4.9 28.0 1.0
O A:HOH720 4.9 17.5 1.0
HE2 A:HIS487 4.9 13.4 1.0
C A:CYS484 4.9 23.0 1.0
HA A:CYS477 5.0 17.1 1.0
O A:HOH762 5.0 12.7 1.0
O A:CYS484 5.0 20.6 1.0

Reference:

J.Kottur, O.Rechkoblit, R.Quintana-Feliciano, D.Sciaky, A.K.Aggarwal. High-Resolution Structures of the Sars-Cov-2 N7-Methyltransferase Inform Therapeutic Development. Nat.Struct.Mol.Biol. V. 29 850 2022.
ISSN: ESSN 1545-9985
PubMed: 36075969
DOI: 10.1038/S41594-022-00828-1
Page generated: Sat Apr 8 03:48:00 2023

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