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Zinc in PDB 1yqn: E. Coli Ispf Double Mutant

Enzymatic activity of E. Coli Ispf Double Mutant

All present enzymatic activity of E. Coli Ispf Double Mutant:
4.6.1.12;

Protein crystallography data

The structure of E. Coli Ispf Double Mutant, PDB code: 1yqn was solved by T.Sgraja, L.E.Kemp, N.Ramsden, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.16 / 3.11
Space group I 21 3
Cell size a, b, c (Å), α, β, γ (°) 143.778, 143.778, 143.778, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 20.9

Other elements in 1yqn:

The structure of E. Coli Ispf Double Mutant also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the E. Coli Ispf Double Mutant (pdb code 1yqn). 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 E. Coli Ispf Double Mutant, PDB code: 1yqn:

Zinc binding site 1 out of 1 in 1yqn

Go back to Zinc Binding Sites List in 1yqn
Zinc binding site 1 out of 1 in the E. Coli Ispf Double Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of E. Coli Ispf Double Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:73.9
occ:1.00
O2B A:CDP200 1.9 78.2 1.0
OD1 A:ASP8 2.0 70.8 1.0
NE2 A:HIS10 2.1 71.5 1.0
ND1 A:HIS42 2.1 68.4 1.0
CG A:ASP8 2.8 69.0 1.0
OD2 A:ASP8 2.9 69.4 1.0
CE1 A:HIS42 2.9 66.8 1.0
CD2 A:HIS10 3.0 70.0 1.0
CE1 A:HIS10 3.0 70.7 1.0
CG A:HIS42 3.2 65.8 1.0
PB A:CDP200 3.2 78.3 1.0
CB A:HIS42 3.6 64.7 1.0
O3B A:CDP200 3.6 78.7 1.0
O1B A:CDP200 4.1 79.4 1.0
ND1 A:HIS10 4.1 70.1 1.0
NE2 A:HIS42 4.1 66.7 1.0
CG A:HIS10 4.1 69.1 1.0
CB A:ASP8 4.2 68.4 1.0
CD2 A:HIS42 4.2 66.4 1.0
O3A A:CDP200 4.4 77.0 1.0
O A:VAL9 4.6 67.7 1.0
CD1 A:ILE57 4.7 85.3 1.0
O A:HOH603 4.7 50.6 1.0

Reference:

T.Sgraja, L.E.Kemp, N.Ramsden, W.N.Hunter. A Double Mutation of Escherichia COLI2C-Methyl-D-Erythritol-2,4-Cyclodiphosphate Synthase Disrupts Six Hydrogen Bonds with, Yet Fails to Prevent Binding of, An Isoprenoid Diphosphate. Acta Crystallogr.,Sect.F V. 61 625 2005.
ISSN: ESSN 1744-3091
PubMed: 16511114
DOI: 10.1107/S1744309105018762
Page generated: Wed Dec 16 03:14:53 2020

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