Atomistry » Zinc » PDB 4lev-4lmy » 4lk1
Atomistry »
  Zinc »
    PDB 4lev-4lmy »
      4lk1 »

Zinc in PDB 4lk1: Crystal Structure Analysis of the E.Coli Holoenzyme

Enzymatic activity of Crystal Structure Analysis of the E.Coli Holoenzyme

All present enzymatic activity of Crystal Structure Analysis of the E.Coli Holoenzyme:
2.7.7.6;

Protein crystallography data

The structure of Crystal Structure Analysis of the E.Coli Holoenzyme, PDB code: 4lk1 was solved by B.Bae, S.A.Darst, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.78 / 3.84
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 186.675, 206.392, 308.836, 90.00, 90.00, 90.00
R / Rfree (%) 22.4 / 27.2

Other elements in 4lk1:

The structure of Crystal Structure Analysis of the E.Coli Holoenzyme also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure Analysis of the E.Coli Holoenzyme (pdb code 4lk1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure Analysis of the E.Coli Holoenzyme, PDB code: 4lk1:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 4lk1

Go back to Zinc Binding Sites List in 4lk1
Zinc binding site 1 out of 4 in the Crystal Structure Analysis of the E.Coli Holoenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure Analysis of the E.Coli Holoenzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1502

b:0.6
occ:1.00
SG D:CYS72 2.2 80.4 1.0
SG D:CYS85 2.3 62.6 1.0
SG D:CYS70 2.3 81.5 1.0
CB D:CYS85 3.1 70.4 1.0
SG D:CYS88 3.4 0.0 1.0
CB D:CYS72 3.5 80.8 1.0
O D:CYS88 3.8 0.9 1.0
CB D:CYS70 3.9 85.2 1.0
CB D:LYS74 4.0 89.9 1.0
N D:CYS72 4.0 0.7 1.0
CB D:LYS87 4.0 0.9 1.0
N D:CYS88 4.0 0.7 1.0
CA D:CYS72 4.2 0.0 1.0
N D:LYS74 4.3 0.6 1.0
N D:GLY73 4.4 0.3 1.0
CA D:CYS85 4.6 99.9 1.0
C D:CYS72 4.7 0.2 1.0
N D:LYS87 4.7 0.2 1.0
C D:CYS88 4.7 0.6 1.0
CB D:CYS88 4.7 0.4 1.0
CA D:CYS88 4.8 0.1 1.0
CA D:LYS87 4.8 0.3 1.0
CA D:LYS74 4.8 96.1 1.0
N D:LEU71 4.8 92.6 1.0
C D:LYS87 4.9 0.9 1.0

Zinc binding site 2 out of 4 in 4lk1

Go back to Zinc Binding Sites List in 4lk1
Zinc binding site 2 out of 4 in the Crystal Structure Analysis of the E.Coli Holoenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure Analysis of the E.Coli Holoenzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1503

b:0.7
occ:1.00
SG D:CYS814 2.3 62.8 1.0
SG D:CYS895 2.3 0.2 1.0
SG D:CYS888 2.3 65.7 1.0
SG D:CYS898 2.4 0.1 1.0
CB D:CYS898 2.7 66.3 1.0
CB D:CYS888 3.0 89.4 1.0
CB D:CYS814 3.5 76.4 1.0
CA D:CYS888 3.5 85.9 1.0
CB D:CYS895 3.8 79.8 1.0
CA D:CYS898 3.9 85.1 1.0
N D:CYS898 4.1 90.6 1.0
NH2 D:ARG883 4.2 0.4 1.0
N D:ASP889 4.2 59.0 1.0
C D:CYS888 4.3 74.8 1.0
N D:CYS814 4.3 69.7 1.0
N D:CYS895 4.4 67.8 1.0
CA D:CYS814 4.5 70.7 1.0
O D:CYS895 4.5 73.5 1.0
CG2 D:THR816 4.5 86.7 1.0
CA D:CYS895 4.6 85.8 1.0
N D:CYS888 4.7 84.3 1.0
C D:CYS895 4.9 65.3 1.0

Zinc binding site 3 out of 4 in 4lk1

Go back to Zinc Binding Sites List in 4lk1
Zinc binding site 3 out of 4 in the Crystal Structure Analysis of the E.Coli Holoenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure Analysis of the E.Coli Holoenzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn1502

b:0.9
occ:1.00
SG J:CYS85 2.2 70.2 1.0
SG J:CYS72 2.2 0.7 1.0
SG J:CYS70 2.3 0.1 1.0
CB J:CYS85 3.1 60.6 1.0
SG J:CYS88 3.4 0.7 1.0
CB J:CYS72 3.5 0.3 1.0
O J:CYS88 3.8 85.2 1.0
CB J:CYS70 3.9 0.2 1.0
CB J:LYS74 4.0 0.1 1.0
N J:CYS72 4.0 0.0 1.0
CB J:LYS87 4.0 89.1 1.0
N J:CYS88 4.0 0.9 1.0
CA J:CYS72 4.2 0.9 1.0
N J:LYS74 4.3 0.0 1.0
N J:GLY73 4.4 0.3 1.0
CA J:CYS85 4.6 84.9 1.0
C J:CYS72 4.7 0.1 1.0
N J:LYS87 4.7 0.7 1.0
C J:CYS88 4.7 99.6 1.0
CB J:CYS88 4.8 0.3 1.0
CA J:CYS88 4.8 0.2 1.0
CA J:LYS74 4.8 0.3 1.0
CA J:LYS87 4.8 0.6 1.0
N J:LEU71 4.8 0.6 1.0
C J:LYS87 4.9 0.6 1.0

Zinc binding site 4 out of 4 in 4lk1

Go back to Zinc Binding Sites List in 4lk1
Zinc binding site 4 out of 4 in the Crystal Structure Analysis of the E.Coli Holoenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure Analysis of the E.Coli Holoenzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn1503

b:37.1
occ:1.00
SG J:CYS814 2.3 83.5 1.0
SG J:CYS895 2.3 52.9 1.0
SG J:CYS888 2.4 73.1 1.0
SG J:CYS898 2.4 88.6 1.0
CB J:CYS898 2.7 63.5 1.0
CB J:CYS888 3.0 87.8 1.0
CB J:CYS814 3.5 75.3 1.0
CA J:CYS888 3.5 50.5 1.0
CB J:CYS895 3.8 89.5 1.0
CA J:CYS898 3.9 78.4 1.0
N J:CYS898 4.1 78.1 1.0
NH2 J:ARG883 4.2 98.2 1.0
N J:ASP889 4.2 73.8 1.0
C J:CYS888 4.3 72.7 1.0
N J:CYS814 4.4 81.1 1.0
N J:CYS895 4.4 95.0 1.0
O J:CYS895 4.5 86.6 1.0
CA J:CYS814 4.5 83.6 1.0
CG2 J:THR816 4.5 97.2 1.0
CA J:CYS895 4.6 92.9 1.0
N J:CYS888 4.7 27.3 1.0
C J:CYS895 4.9 82.9 1.0

Reference:

B.Bae, E.Davis, D.Brown, E.A.Campbell, S.Wigneshweraraj, S.A.Darst. Phage T7 GP2 Inhibition of Escherichia Coli Rna Polymerase Involves Misappropriation of Sigma 70 Domain 1.1. Proc.Natl.Acad.Sci.Usa V. 110 19772 2013.
ISSN: ISSN 0027-8424
PubMed: 24218560
DOI: 10.1073/PNAS.1314576110
Page generated: Sun Oct 27 01:54:35 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy