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Zinc in PDB 4f9v: Structure of C113A/C136A Mutant Variant of Glycosylated Glutaminyl Cyclase From Drosophila Melanogaster

Enzymatic activity of Structure of C113A/C136A Mutant Variant of Glycosylated Glutaminyl Cyclase From Drosophila Melanogaster

All present enzymatic activity of Structure of C113A/C136A Mutant Variant of Glycosylated Glutaminyl Cyclase From Drosophila Melanogaster:
2.3.2.5;

Protein crystallography data

The structure of Structure of C113A/C136A Mutant Variant of Glycosylated Glutaminyl Cyclase From Drosophila Melanogaster, PDB code: 4f9v was solved by P.Kolenko, B.Koch, D.Ruiz-Carilo, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.10
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 170.865, 170.865, 57.236, 90.00, 90.00, 120.00
R / Rfree (%) 17.4 / 21.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of C113A/C136A Mutant Variant of Glycosylated Glutaminyl Cyclase From Drosophila Melanogaster (pdb code 4f9v). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of C113A/C136A Mutant Variant of Glycosylated Glutaminyl Cyclase From Drosophila Melanogaster, PDB code: 4f9v:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4f9v

Go back to Zinc Binding Sites List in 4f9v
Zinc binding site 1 out of 2 in the Structure of C113A/C136A Mutant Variant of Glycosylated Glutaminyl Cyclase From Drosophila Melanogaster


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of C113A/C136A Mutant Variant of Glycosylated Glutaminyl Cyclase From Drosophila Melanogaster within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:17.3
occ:1.00
OE2 A:GLU171 1.9 14.1 1.0
NAM A:PBD402 1.9 18.4 1.0
OD2 A:ASP131 2.0 15.6 1.0
NE2 A:HIS297 2.1 22.1 1.0
CD A:GLU171 2.7 20.2 1.0
CG A:ASP131 2.8 17.4 1.0
OD1 A:ASP131 2.9 15.9 1.0
CAD A:PBD402 2.9 18.5 1.0
CAH A:PBD402 2.9 17.0 1.0
OE1 A:GLU171 2.9 20.7 1.0
CD2 A:HIS297 3.0 20.0 1.0
CE1 A:HIS297 3.2 20.4 1.0
NE1 A:TRP296 3.7 20.7 1.0
O A:HOH575 4.0 14.2 1.0
NAV A:PBD402 4.1 19.8 1.0
CAG A:PBD402 4.1 19.9 1.0
CG A:GLU171 4.1 16.9 1.0
CB A:ASP131 4.2 17.7 1.0
CG A:HIS297 4.2 20.1 1.0
ND1 A:HIS297 4.3 20.0 1.0
OE1 A:GLU170 4.4 20.6 1.0
CE2 A:TRP296 4.5 19.6 1.0
CD1 A:TRP296 4.5 19.0 1.0
O A:HOH503 4.6 14.2 1.0
CZ2 A:TRP296 4.7 20.4 1.0
NE2 A:HIS114 4.7 12.1 1.0
CD A:LYS118 4.8 18.4 1.0
O A:ASP131 5.0 17.5 1.0
CB A:LYS118 5.0 17.0 1.0

Zinc binding site 2 out of 2 in 4f9v

Go back to Zinc Binding Sites List in 4f9v
Zinc binding site 2 out of 2 in the Structure of C113A/C136A Mutant Variant of Glycosylated Glutaminyl Cyclase From Drosophila Melanogaster


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of C113A/C136A Mutant Variant of Glycosylated Glutaminyl Cyclase From Drosophila Melanogaster within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:19.6
occ:1.00
OE2 B:GLU171 1.9 18.5 1.0
NE2 B:HIS297 2.0 15.5 1.0
OD2 B:ASP131 2.0 15.7 1.0
NAM B:PBD402 2.1 19.7 1.0
CD B:GLU171 2.7 19.2 1.0
CG B:ASP131 2.8 17.6 1.0
OE1 B:GLU171 2.8 18.7 1.0
OD1 B:ASP131 2.9 19.8 1.0
CD2 B:HIS297 3.0 17.2 1.0
CE1 B:HIS297 3.0 16.4 1.0
CAD B:PBD402 3.0 17.6 1.0
CAH B:PBD402 3.1 18.7 1.0
NE1 B:TRP296 3.8 14.3 1.0
O B:HOH516 4.0 17.3 1.0
ND1 B:HIS297 4.1 15.9 1.0
CG B:HIS297 4.1 16.8 1.0
CG B:GLU171 4.1 18.9 1.0
CAG B:PBD402 4.2 20.2 1.0
NAV B:PBD402 4.2 19.8 1.0
CB B:ASP131 4.2 19.1 1.0
OE1 B:GLU170 4.4 21.2 1.0
O B:HOH513 4.5 14.9 1.0
CD1 B:TRP296 4.6 16.1 1.0
CE2 B:TRP296 4.6 15.5 1.0
NE2 B:HIS114 4.7 18.1 1.0
CD B:LYS118 4.8 19.8 1.0
CE1 B:HIS114 4.9 18.7 1.0
CZ2 B:TRP296 4.9 18.0 1.0
O B:HOH525 5.0 18.9 1.0
O B:ASP131 5.0 19.5 1.0
CB B:LYS118 5.0 19.1 1.0

Reference:

B.Koch, P.Kolenko, M.Buchholz, D.Ruiz Carrillo, C.Parthier, M.Wermann, J.U.Rahfeld, G.Reuter, S.Schilling, M.T.Stubbs, H.U.Demuth. Crystal Structures of Glutaminyl Cyclases (Qcs) From Drosophila Melanogaster Reveal Active Site Conservation Between Insect and Mammalian Qcs. Biochemistry V. 51 7383 2012.
ISSN: ISSN 0006-2960
PubMed: 22897232
DOI: 10.1021/BI300687G
Page generated: Wed Dec 16 05:17:12 2020

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