Zinc in PDB 7apm: Trna-Guanine Transglycosylase H319C Mutant Spin-Labeled with Mtsl

Enzymatic activity of Trna-Guanine Transglycosylase H319C Mutant Spin-Labeled with Mtsl

All present enzymatic activity of Trna-Guanine Transglycosylase H319C Mutant Spin-Labeled with Mtsl:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase H319C Mutant Spin-Labeled with Mtsl, PDB code: 7apm was solved by D.Nguyen, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.68 / 1.66
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.911, 65.064, 70.813, 90.00, 96.29, 90.00
R / Rfree (%) 13.9 / 17.6

Other elements in 7apm:

The structure of Trna-Guanine Transglycosylase H319C Mutant Spin-Labeled with Mtsl also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase H319C Mutant Spin-Labeled with Mtsl (pdb code 7apm). 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 Trna-Guanine Transglycosylase H319C Mutant Spin-Labeled with Mtsl, PDB code: 7apm:

Zinc binding site 1 out of 1 in 7apm

Go back to Zinc Binding Sites List in 7apm
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase H319C Mutant Spin-Labeled with Mtsl


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Trna-Guanine Transglycosylase H319C Mutant Spin-Labeled with Mtsl within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:17.4
occ:1.00
ND1 A:HIS349 2.1 16.0 1.0
SG A:CYS320 2.3 16.1 1.0
SG A:CYS318 2.3 18.3 1.0
SG A:CYS323 2.3 17.0 1.0
CE1 A:HIS349 2.9 16.9 1.0
HE1 A:HIS349 2.9 20.3 1.0
HB3 A:CYS318 3.1 20.7 1.0
HB2 A:CYS323 3.1 20.4 1.0
HB3 A:CYS320 3.2 17.3 1.0
CG A:HIS349 3.3 15.0 1.0
CB A:CYS318 3.3 17.3 1.0
CB A:CYS323 3.3 17.0 1.0
H A:CYS323 3.3 20.0 1.0
HB2 A:HIS349 3.4 17.7 1.0
CB A:CYS320 3.4 14.4 1.0
H A:CYS320 3.5 20.8 1.0
HA A:HIS349 3.5 14.2 1.0
HB2 A:CYS318 3.7 20.7 1.0
CB A:HIS349 3.7 14.8 1.0
HB A:VAL322 3.9 18.9 1.0
N A:CYS323 3.9 16.7 1.0
HB3 A:CYS323 4.0 20.4 1.0
NE2 A:HIS349 4.1 15.3 1.0
CA A:HIS349 4.1 11.9 1.0
HB2 A:CYS320 4.1 17.3 1.0
N A:CYS320 4.2 17.3 1.0
HB2 A:LEU314 4.2 18.8 1.0
CA A:CYS323 4.2 17.3 1.0
CA A:CYS320 4.2 17.0 1.0
CD2 A:HIS349 4.3 15.5 1.0
HB3 A:ASP315 4.5 23.9 1.0
HB3 A:ALA352 4.5 17.5 1.0
HE22 A:GLN356 4.5 29.9 1.0
HD12 A:LEU314 4.6 18.5 1.0
O A:HIS349 4.6 13.9 1.0
HA A:CYS323 4.6 20.8 1.0
H A:ASP315 4.6 21.6 1.0
CA A:CYS318 4.6 18.6 1.0
HB3 A:HIS349 4.6 17.7 1.0
O A:CYS320 4.6 16.6 1.0
C A:CYS320 4.7 16.6 1.0
C A:CYS318 4.7 19.6 1.0
H A:VAL322 4.7 19.1 1.0
C A:HIS349 4.8 13.2 1.0
HE2 A:HIS349 4.8 18.3 1.0
CB A:VAL322 4.8 15.8 1.0
O A:CYS318 4.9 20.5 1.0
C A:VAL322 5.0 17.9 1.0

Reference:

D.Abdullin, D.Nguyen, C.A.Heubach, A.Nguyen, T.Pfaffeneder, A.Heine, K.Reuter, F.Diederich, O.Schiemann, G.Klebe. Unraveling A Ligand-Induced Twist of A Homodimeric Enzyme By Pulsed Electron-Electron Double Resonance To Be Published.
Page generated: Wed Dec 16 13:35:33 2020

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