Zinc in PDB 7pvm: uc(Nmr) Structure of the C. Thermophilum XRN2 Zinc Finger

Zinc Binding Sites:

The binding sites of Zinc atom in the uc(Nmr) Structure of the C. Thermophilum XRN2 Zinc Finger (pdb code 7pvm). 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 uc(Nmr) Structure of the C. Thermophilum XRN2 Zinc Finger, PDB code: 7pvm:

Zinc binding site 1 out of 1 in 7pvm

Go back to Zinc Binding Sites List in 7pvm
Zinc binding site 1 out of 1 in the uc(Nmr) Structure of the C. Thermophilum XRN2 Zinc Finger


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of uc(Nmr) Structure of the C. Thermophilum XRN2 Zinc Finger within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn101

b:3.4
occ:1.00
SG A:CYS12 2.0 72.0 1.0
NE2 A:HIS17 2.2 11.3 1.0
SG A:CYS22 2.3 22.1 1.0
SG A:CYS9 2.3 42.1 1.0
HB2 A:CYS12 2.3 24.4 1.0
CB A:CYS12 2.6 64.4 1.0
CD2 A:HIS17 2.9 13.2 1.0
HD2 A:HIS17 2.9 35.4 1.0
HB3 A:CYS9 3.1 32.2 1.0
H A:CYS12 3.1 61.0 1.0
CB A:CYS9 3.1 4.4 1.0
HB2 A:CYS9 3.2 44.1 1.0
HB2 A:CYS22 3.3 21.3 1.0
CB A:CYS22 3.4 30.1 1.0
CE1 A:HIS17 3.4 70.2 1.0
HB3 A:CYS12 3.5 3.5 1.0
N A:CYS12 3.5 20.1 1.0
CA A:CYS12 3.6 72.3 1.0
HB3 A:CYS22 3.7 44.1 1.0
HE1 A:HIS17 3.8 14.3 1.0
HB2 A:LEU11 3.8 23.1 1.0
CG A:HIS17 4.1 52.3 1.0
H A:LEU11 4.2 73.4 1.0
HA A:CYS12 4.2 14.5 1.0
HG A:LEU11 4.2 1.4 1.0
ND1 A:HIS17 4.3 11.1 1.0
C A:LEU11 4.4 61.0 1.0
HA A:GLU19 4.4 11.3 1.0
HD11 A:LEU11 4.4 41.4 1.0
H A:GLY13 4.5 43.2 1.0
CA A:CYS9 4.5 73.2 1.0
CB A:LEU11 4.6 41.4 1.0
O A:ASP18 4.6 10.2 1.0
CA A:CYS22 4.7 71.1 1.0
HA A:CYS22 4.7 41.4 1.0
C A:CYS12 4.8 54.4 1.0
CG A:LEU11 4.8 14.4 1.0
HA A:CYS9 4.8 54.3 1.0
N A:LEU11 4.9 24.2 1.0
CA A:LEU11 4.9 45.2 1.0
H A:GLN14 5.0 51.4 1.0

Reference:

J.H.Overbeck, D.Stelzig, A.L.Fuchs, J.P.Wurm, R.Sprangers. Observation of Conformational Changes That Underlie the Catalytic Cycle of XRN2. Nat.Chem.Biol. V. 18 1152 2022.
ISSN: ESSN 1552-4469
PubMed: 36008487
DOI: 10.1038/S41589-022-01111-6
Page generated: Sat Apr 8 01:40:24 2023

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