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Zinc in PDB 5f6c: The Structure of E. Coli Rnase E Catalytically Inactive Mutant with Rna Bound

Enzymatic activity of The Structure of E. Coli Rnase E Catalytically Inactive Mutant with Rna Bound

All present enzymatic activity of The Structure of E. Coli Rnase E Catalytically Inactive Mutant with Rna Bound:
3.1.26.12;

Protein crystallography data

The structure of The Structure of E. Coli Rnase E Catalytically Inactive Mutant with Rna Bound, PDB code: 5f6c was solved by K.J.Bandyra, B.F.Luisi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 54.62 / 3.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.619, 122.562, 122.195, 90.00, 99.77, 90.00
R / Rfree (%) 17.5 / 25

Other elements in 5f6c:

The structure of The Structure of E. Coli Rnase E Catalytically Inactive Mutant with Rna Bound also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the The Structure of E. Coli Rnase E Catalytically Inactive Mutant with Rna Bound (pdb code 5f6c). 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 The Structure of E. Coli Rnase E Catalytically Inactive Mutant with Rna Bound, PDB code: 5f6c:

Zinc binding site 1 out of 1 in 5f6c

Go back to Zinc Binding Sites List in 5f6c
Zinc binding site 1 out of 1 in the The Structure of E. Coli Rnase E Catalytically Inactive Mutant with Rna Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of E. Coli Rnase E Catalytically Inactive Mutant with Rna Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn602

b:90.2
occ:1.00
 HG A:CYS407 1.3 0.3 1.0
SG A:CYS407 2.1 96.9 1.0
SG A:CYS404 2.1 86.5 1.0
SG B:CYS404 2.2 82.3 1.0
SG B:CYS407 2.6 89.9 1.0
HB3 A:CYS404 2.9 93.5 1.0
CB A:CYS404 3.0 78.0 1.0
H A:CYS407 3.0 0.5 1.0
HB3 B:CYS404 3.2 98.5 1.0
HB2 A:CYS404 3.2 93.5 1.0
CB B:CYS404 3.3 82.0 1.0
HB3 A:CYS407 3.4 0.2 1.0
H B:CYS407 3.4 0.3 1.0
CB A:CYS407 3.4 88.5 1.0
HB2 B:ARG406 3.5 0.3 1.0
HB2 B:CYS404 3.5 98.5 1.0
N A:CYS407 3.8 96.2 1.0
HB3 A:ARG406 3.9 82.4 1.0
CB B:CYS407 4.0 96.3 1.0
HB3 B:CYS407 4.1 0.6 1.0
HB2 A:CYS407 4.1 0.2 1.0
O B:CYS407 4.1 97.1 1.0
N B:CYS407 4.1 90.2 1.0
CA A:CYS407 4.2 90.4 1.0
H B:GLY411 4.2 79.9 1.0
H A:ARG406 4.4 82.0 1.0
O A:THR410 4.4 88.8 1.0
CB B:ARG406 4.4 89.4 1.0
CA A:CYS404 4.4 73.1 1.0
HA2 B:GLY411 4.4 92.0 1.0
H B:ARG406 4.5 92.3 1.0
CA B:CYS407 4.6 89.6 1.0
CA B:CYS404 4.6 66.6 1.0
HA2 A:GLY411 4.7 91.8 1.0
HG2 B:ARG406 4.7 0.2 1.0
HA A:CYS404 4.8 87.7 1.0
C B:CYS407 4.8 86.4 1.0
HB2 B:CYS407 4.8 0.6 1.0
CB A:ARG406 4.8 68.7 1.0
HG3 B:ARG406 4.8 0.2 1.0
C A:CYS404 4.9 84.6 1.0
H B:GLY409 4.9 0.9 1.0
H A:SER408 4.9 0.3 1.0
N B:ARG406 4.9 76.9 1.0
C A:ARG406 4.9 87.8 1.0
HB3 B:ARG406 4.9 0.3 1.0
C B:CYS404 4.9 74.6 1.0
N B:GLY411 4.9 66.6 1.0
N A:ARG406 4.9 68.4 1.0
C A:CYS407 5.0 82.4 1.0
CG B:ARG406 5.0 0.1 1.0
HA A:CYS407 5.0 0.4 1.0

Reference:

K.J.Bandyra, J.M.Wandzik, B.F.Luisi. Substrate Recognition and Autoinhibition in the Central Ribonuclease Rnase E. Mol. Cell V. 72 275 2018.
ISSN: ISSN 1097-4164
PubMed: 30270108
DOI: 10.1016/J.MOLCEL.2018.08.039
Page generated: Sun Oct 27 15:49:17 2024

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