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Zinc in PDB 1fj6: Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State)

Enzymatic activity of Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State)

All present enzymatic activity of Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State):
3.1.3.11;

Protein crystallography data

The structure of Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State), PDB code: 1fj6 was solved by C.V.Iancu, J.Y.Choe, R.B.Honzatko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 2.50
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 52.380, 82.470, 165.590, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 27.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State) (pdb code 1fj6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State), PDB code: 1fj6:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 1fj6

Go back to Zinc Binding Sites List in 1fj6
Zinc binding site 1 out of 3 in the Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:26.3
occ:1.00
O A:LEU120 2.0 14.4 1.0
OD2 A:ASP118 2.1 28.6 1.0
OE1 A:GLU97 2.3 15.8 1.0
O1 A:PO4402 2.3 20.1 1.0
O3 A:PO4402 2.5 25.0 1.0
P A:PO4402 2.9 25.2 1.0
C A:LEU120 3.1 17.9 1.0
CG A:ASP118 3.2 26.0 1.0
CD A:GLU97 3.2 15.1 1.0
OD1 A:ASP118 3.6 35.5 1.0
O2 A:PO4402 3.7 21.3 1.0
N A:LEU120 3.8 20.1 1.0
ZN A:ZN404 3.9 27.7 1.0
ZN A:ZN405 3.9 33.8 1.0
OE2 A:GLU97 3.9 13.7 1.0
N A:ASP121 3.9 20.5 1.0
CA A:LEU120 3.9 21.0 1.0
OE1 A:GLU98 4.0 31.5 1.0
CA A:ASP121 4.1 21.7 1.0
O4 A:PO4402 4.1 23.0 1.0
CG A:GLU97 4.2 18.1 1.0
OD2 A:ASP74 4.3 31.2 1.0
CB A:ASP118 4.5 24.5 1.0
CB A:LEU120 4.5 21.9 1.0
CD A:PRO119 4.6 19.2 1.0
C A:ASP118 4.6 21.5 1.0
CA A:ASP118 4.6 19.8 1.0
N A:PRO119 4.7 19.6 1.0
CB A:GLU97 4.8 22.4 1.0
NH2 A:ARG276 4.9 22.7 1.0
C A:PRO119 5.0 19.4 1.0
CB A:ASP121 5.0 22.2 1.0

Zinc binding site 2 out of 3 in 1fj6

Go back to Zinc Binding Sites List in 1fj6
Zinc binding site 2 out of 3 in the Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn404

b:27.7
occ:1.00
OD1 A:ASP118 1.9 35.5 1.0
O1 A:PO4402 2.1 20.1 1.0
OD1 A:ASP121 2.1 26.1 1.0
OE1 A:GLU280 2.2 31.9 1.0
CG A:ASP118 3.0 26.0 1.0
CG A:ASP121 3.1 28.0 1.0
CD A:GLU280 3.1 25.9 1.0
CB A:ASP121 3.3 22.2 1.0
P A:PO4402 3.3 25.2 1.0
OD2 A:ASP118 3.4 28.6 1.0
CA A:ASP121 3.5 21.7 1.0
CG A:GLU280 3.5 23.5 1.0
O4 A:PO4402 3.5 23.0 1.0
ZN A:ZN403 3.9 26.3 1.0
NH2 A:ARG276 3.9 22.7 1.0
OE1 A:GLU97 4.0 15.8 1.0
C1 A:F6P401 4.1 15.9 1.0
O2 A:PO4402 4.1 21.3 1.0
CB A:ASP118 4.2 24.5 1.0
OD2 A:ASP121 4.2 25.6 1.0
OE2 A:GLU280 4.3 29.5 1.0
O A:LEU120 4.3 14.4 1.0
O3 A:F6P401 4.4 13.6 1.0
N A:GLY122 4.4 20.7 1.0
O3 A:PO4402 4.4 25.0 1.0
CD1 A:ILE135 4.4 10.9 1.0
C A:ASP121 4.5 22.8 1.0
N A:ASP121 4.5 20.5 1.0
O1 A:F6P401 4.6 16.2 1.0
O2 A:F6P401 4.7 21.1 1.0
C2 A:F6P401 4.8 18.7 1.0
C A:LEU120 4.8 17.9 1.0
C3 A:F6P401 4.8 17.7 1.0
CB A:GLU280 4.9 18.5 1.0
CD A:GLU97 5.0 15.1 1.0

Zinc binding site 3 out of 3 in 1fj6

Go back to Zinc Binding Sites List in 1fj6
Zinc binding site 3 out of 3 in the Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn405

b:33.8
occ:1.00
O2 A:PO4402 1.9 21.3 1.0
OD2 A:ASP68 2.2 28.3 1.0
OE2 A:GLU97 2.4 13.7 1.0
O3 A:PO4402 2.8 25.0 1.0
P A:PO4402 2.9 25.2 1.0
CD A:GLU97 3.1 15.1 1.0
CG A:ASP68 3.1 30.7 1.0
CB A:ASP68 3.4 31.8 1.0
OE1 A:GLU97 3.5 15.8 1.0
O1 A:PO4402 3.7 20.1 1.0
ND2 A:ASN64 3.8 28.8 1.0
NH2 A:ARG276 3.8 22.7 1.0
ZN A:ZN403 3.9 26.3 1.0
OE1 A:GLU98 3.9 31.5 1.0
O4 A:PO4402 4.1 23.0 1.0
CG A:GLU97 4.2 18.1 1.0
OD1 A:ASP68 4.3 31.5 1.0
NH1 A:ARG276 4.3 22.3 1.0
CZ A:ARG276 4.6 25.5 1.0
O1 A:F6P401 4.8 16.2 1.0
CB A:SER123 4.8 19.8 1.0
CA A:ASP68 5.0 35.4 1.0
OG A:SER123 5.0 24.3 1.0

Reference:

S.W.Nelson, C.V.Iancu, J.Y.Choe, R.B.Honzatko, H.J.Fromm. Tryptophan Fluorescence Reveals the Conformational State of A Dynamic Loop in Recombinant Porcine Fructose-1,6-Bisphosphatase. Biochemistry V. 39 11100 2000.
ISSN: ISSN 0006-2960
PubMed: 10998248
DOI: 10.1021/BI000609C
Page generated: Wed Dec 16 02:49:13 2020

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