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Zinc in PDB 6g63: Rnase E in Complex with Srna Rrpa

Enzymatic activity of Rnase E in Complex with Srna Rrpa

All present enzymatic activity of Rnase E in Complex with Srna Rrpa:
3.1.26.12;

Protein crystallography data

The structure of Rnase E in Complex with Srna Rrpa, PDB code: 6g63 was solved by K.B.Bandyra, B.F.Luisi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.95 / 3.95
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 110.630, 110.630, 466.020, 90.00, 90.00, 120.00
R / Rfree (%) 27.5 / 29.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Rnase E in Complex with Srna Rrpa (pdb code 6g63). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Rnase E in Complex with Srna Rrpa, PDB code: 6g63:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6g63

Go back to Zinc Binding Sites List in 6g63
Zinc binding site 1 out of 2 in the Rnase E in Complex with Srna Rrpa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Rnase E in Complex with Srna Rrpa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:0.1
occ:1.00
SG A:CYS404 2.1 0.8 1.0
SG G:CYS404 2.2 0.4 1.0
SG A:CYS407 2.4 0.6 1.0
SG G:CYS407 2.5 0.3 1.0
CB A:CYS404 3.2 0.5 1.0
HB3 G:CYS407 3.2 0.7 1.0
H G:CYS407 3.2 0.7 1.0
HB2 A:CYS404 3.3 0.7 1.0
HB3 A:CYS404 3.3 0.7 1.0
HB3 A:CYS407 3.3 0.7 1.0
HB3 G:CYS404 3.3 0.7 1.0
CB G:CYS404 3.3 0.2 1.0
H A:CYS407 3.3 0.7 1.0
HB2 G:CYS404 3.4 0.7 1.0
CB G:CYS407 3.5 0.2 1.0
CB A:CYS407 3.5 0.9 1.0
HB3 G:ARG406 3.8 0.7 1.0
HB3 A:ARG406 3.8 0.7 1.0
HA2 A:GLY411 3.9 0.7 1.0
HA2 G:GLY411 3.9 0.7 1.0
N G:CYS407 4.0 0.8 1.0
N A:CYS407 4.1 0.9 1.0
H A:GLY411 4.1 0.7 1.0
H G:GLY411 4.2 0.7 1.0
HB2 A:CYS407 4.2 0.7 1.0
HB2 G:CYS407 4.2 0.7 1.0
CA G:CYS407 4.4 0.3 1.0
CA A:CYS407 4.4 1.0 1.0
H A:GLY409 4.4 0.7 1.0
H G:GLY409 4.5 0.7 1.0
H G:ARG406 4.5 0.7 1.0
CA A:CYS404 4.6 0.9 1.0
H A:ARG406 4.6 0.7 1.0
CA G:CYS404 4.7 0.8 1.0
CA A:GLY411 4.7 1.0 1.0
CA G:GLY411 4.7 0.6 1.0
CB G:ARG406 4.8 0.1 1.0
N A:GLY411 4.8 0.5 1.0
CB A:ARG406 4.8 0.8 1.0
N G:GLY411 4.8 0.3 1.0
HA A:CYS404 4.9 0.7 1.0
HA2 G:GLY409 4.9 0.7 1.0
HD3 A:ARG406 4.9 0.7 1.0
HA G:CYS404 5.0 0.7 1.0

Zinc binding site 2 out of 2 in 6g63

Go back to Zinc Binding Sites List in 6g63
Zinc binding site 2 out of 2 in the Rnase E in Complex with Srna Rrpa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Rnase E in Complex with Srna Rrpa within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Zn601

b:0.1
occ:1.00
SG N:CYS404 2.2 0.4 1.0
SG L:CYS404 2.3 1.0 1.0
SG L:CYS407 2.5 0.6 1.0
HB3 N:CYS407 2.6 0.7 1.0
SG N:CYS407 2.6 0.7 1.0
HB3 L:CYS407 2.7 0.7 1.0
H N:CYS407 3.0 0.7 1.0
H L:CYS407 3.0 0.7 1.0
CB N:CYS407 3.1 0.3 1.0
CB L:CYS407 3.2 0.7 1.0
HB3 L:ARG406 3.3 0.7 1.0
CB N:CYS404 3.3 0.0 1.0
HB3 L:CYS404 3.3 0.7 1.0
HB3 N:CYS404 3.3 0.7 1.0
CB L:CYS404 3.4 0.6 1.0
HB2 N:CYS404 3.4 0.7 1.0
HB2 L:CYS404 3.6 0.7 1.0
HB3 N:ARG406 3.6 0.7 1.0
N N:CYS407 3.7 1.0 1.0
N L:CYS407 3.7 0.4 1.0
HB2 N:CYS407 3.8 0.7 1.0
HB2 L:CYS407 3.9 0.7 1.0
CA N:CYS407 4.0 0.8 1.0
CA L:CYS407 4.1 0.1 1.0
HA2 L:GLY411 4.1 0.7 1.0
HD3 L:ARG406 4.2 0.7 1.0
CB L:ARG406 4.2 0.3 1.0
HA2 N:GLY411 4.3 0.7 1.0
H L:GLY411 4.3 0.7 1.0
H L:ARG406 4.4 0.7 1.0
H N:ARG406 4.5 0.7 1.0
H N:GLY411 4.5 0.7 1.0
H L:GLY409 4.6 0.7 1.0
CB N:ARG406 4.6 0.3 1.0
HB2 L:ARG406 4.7 0.7 1.0
HA N:CYS407 4.7 0.7 1.0
CA N:CYS404 4.7 0.7 1.0
HD3 N:ARG406 4.7 0.7 1.0
H N:GLY409 4.7 0.7 1.0
C L:ARG406 4.7 0.9 1.0
HG2 L:ARG406 4.8 0.7 1.0
CA L:CYS404 4.8 0.7 1.0
HA L:CYS407 4.8 0.7 1.0
C N:ARG406 4.8 0.5 1.0
CA L:ARG406 4.9 0.6 1.0
CA L:GLY411 4.9 0.6 1.0
N L:ARG406 4.9 0.2 1.0
CG L:ARG406 4.9 0.1 1.0
N L:GLY411 4.9 0.7 1.0
HA N:CYS404 5.0 0.7 1.0
C N:CYS407 5.0 0.1 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: Mon Oct 28 21:39:53 2024

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