Zinc in PDB 4av7: Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1

The structure of Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1, PDB code: 4av7 was solved by T.Knaus, M.Schober, K.Faber, P.Macharaux, U.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.65 / 3.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	75.201, 201.955, 248.495, 90.00, 90.00, 90.00
R / Rfree (%)	18.646 / 25.591

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Zinc atom in the Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1 (pdb code 4av7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 12 binding sites of Zinc where determined in the Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1, PDB code: 4av7:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 12 in the Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn700 b:53.9 occ:1.00 NE2 A:HIS184 1.9 50.0 1.0 NE2 A:HIS355 2.0 51.2 1.0 OD2 A:ASP310 2.0 57.9 1.0 OD2 A:ASP183 2.1 59.7 1.0 CD2 A:HIS355 2.8 47.3 1.0 O A:HOH2029 2.8 37.6 1.0 CE1 A:HIS184 2.9 52.8 1.0 CD2 A:HIS184 3.0 54.0 1.0 CG A:ASP183 3.1 59.8 1.0 ZN A:ZN701 3.1 47.8 1.0 CG A:ASP310 3.1 58.0 1.0 CE1 A:HIS355 3.1 54.8 1.0 OD1 A:ASP183 3.4 59.5 1.0 OD1 A:ASP310 3.5 61.1 1.0 NE2 A:HIS179 3.7 50.6 1.0 ND1 A:HIS184 4.0 53.6 1.0 CG A:HIS355 4.1 51.3 1.0 CE1 A:HIS179 4.1 52.1 1.0 CG A:HIS184 4.1 54.5 1.0 ND1 A:HIS355 4.2 54.6 1.0 CB A:ASP183 4.4 62.7 1.0 CB A:ASP310 4.4 53.1 1.0 OE2 A:GLU291 4.5 68.3 1.0 CB A:ALA133 4.6 48.7 1.0 ND1 A:HIS181 4.7 50.0 1.0 CB A:HIS181 4.8 54.7 1.0 CD2 A:HIS179 4.9 51.6 1.0

Zinc binding site 2 out of 12 in the Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:47.8 occ:1.00 OE2 A:GLU291 1.9 68.3 1.0 ND1 A:HIS181 2.2 50.0 1.0 NE2 A:HIS179 2.2 50.6 1.0 OD2 A:ASP310 2.3 57.9 1.0 CD A:GLU291 2.7 64.1 1.0 OE1 A:GLU291 2.8 59.0 1.0 O A:HOH2029 2.9 37.6 1.0 CD2 A:HIS179 2.9 51.6 1.0 CE1 A:HIS181 3.1 49.7 1.0 ZN A:ZN700 3.1 53.9 1.0 CG A:HIS181 3.2 52.1 1.0 CE1 A:HIS179 3.2 52.1 1.0 CG A:ASP310 3.3 58.0 1.0 CB A:HIS181 3.6 54.7 1.0 CB A:ASP310 3.6 53.1 1.0 NE2 A:HIS184 3.7 50.0 1.0 CG A:HIS179 4.1 55.0 1.0 CD2 A:HIS184 4.1 54.0 1.0 CG A:GLU291 4.2 56.4 1.0 ND1 A:HIS179 4.2 54.5 1.0 NE2 A:HIS181 4.2 54.7 1.0 CD2 A:HIS181 4.3 51.8 1.0 OD1 A:ASP310 4.3 61.1 1.0 OD1 A:ASP183 4.4 59.5 1.0 OD2 A:ASP183 4.5 59.7 1.0 NE2 A:HIS317 4.5 42.6 1.0 O2 A:SO4801 4.7 59.9 1.0 CE1 A:HIS184 4.7 52.8 1.0 NE2 A:HIS355 4.8 51.2 1.0 CG A:ASP183 4.9 59.8 1.0 O1 A:SO4801 4.9 60.5 1.0

Zinc binding site 3 out of 12 in the Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn700 b:64.3 occ:1.00 NE2 B:HIS184 1.9 89.2 1.0 OD2 B:ASP183 2.0 84.3 1.0 OD2 B:ASP310 2.0 82.1 1.0 NE2 B:HIS355 2.1 50.9 1.0 CD2 B:HIS355 2.9 47.1 1.0 CD2 B:HIS184 2.9 98.3 1.0 CE1 B:HIS184 3.0 90.3 1.0 CG B:ASP310 3.0 76.5 1.0 CG B:ASP183 3.0 82.1 1.0 ZN B:ZN701 3.1 70.4 1.0 OD1 B:ASP310 3.3 72.0 1.0 CE1 B:HIS355 3.3 52.0 1.0 OD1 B:ASP183 3.4 84.0 1.0 NE2 B:HIS179 3.6 70.0 1.0 CE1 B:HIS179 3.8 69.6 1.0 ND1 B:HIS184 4.1 94.2 1.0 CG B:HIS184 4.1 97.3 1.0 CG B:HIS355 4.1 47.0 1.0 ND1 B:HIS355 4.3 49.2 1.0 CB B:ASP183 4.3 87.3 1.0 CB B:ASP310 4.4 70.4 1.0 ND1 B:HIS181 4.8 0.1 1.0 CB B:ALA133 4.8 66.6 1.0 CD2 B:HIS179 4.9 74.9 1.0 OE2 B:GLU291 4.9 82.9 1.0 CB B:HIS181 5.0 97.7 1.0

Zinc binding site 4 out of 12 in the Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:70.4 occ:1.00 NE2 B:HIS179 1.9 70.0 1.0 ND1 B:HIS181 2.2 0.1 1.0 OD2 B:ASP310 2.4 82.1 1.0 OE2 B:GLU291 2.5 82.9 1.0 CD2 B:HIS179 2.7 74.9 1.0 OE1 B:GLU291 2.8 86.7 1.0 CD B:GLU291 3.0 86.2 1.0 CE1 B:HIS179 3.0 69.6 1.0 ZN B:ZN700 3.1 64.3 1.0 CE1 B:HIS181 3.1 0.2 1.0 CG B:HIS181 3.2 97.7 1.0 CG B:ASP310 3.2 76.5 1.0 CB B:HIS181 3.6 97.7 1.0 CB B:ASP310 3.6 70.4 1.0 NE2 B:HIS184 3.8 89.2 1.0 CG B:HIS179 3.9 76.5 1.0 ND1 B:HIS179 4.0 73.8 1.0 CD2 B:HIS184 4.1 98.3 1.0 NE2 B:HIS181 4.2 0.4 1.0 OD1 B:ASP183 4.3 84.0 1.0 OD1 B:ASP310 4.3 72.0 1.0 CD2 B:HIS181 4.3 0.6 1.0 OD2 B:ASP183 4.4 84.3 1.0 CG B:GLU291 4.5 80.2 1.0 NE2 B:HIS317 4.7 61.6 1.0 CG B:ASP183 4.8 82.1 1.0 O2 B:SO4801 4.8 90.7 1.0 CE1 B:HIS184 4.9 90.3 1.0 NE2 B:HIS355 5.0 50.9 1.0

Zinc binding site 5 out of 12 in the Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn700 b:68.5 occ:1.00 OD2 C:ASP310 2.0 76.5 1.0 NE2 C:HIS184 2.0 70.5 1.0 OD2 C:ASP183 2.0 79.3 1.0 NE2 C:HIS355 2.2 83.2 1.0 CD2 C:HIS355 2.9 80.7 1.0 CG C:ASP183 2.9 74.9 1.0 CD2 C:HIS184 3.0 69.5 1.0 CE1 C:HIS184 3.0 71.6 1.0 CG C:ASP310 3.1 70.7 1.0 ZN C:ZN701 3.1 50.2 1.0 OD1 C:ASP183 3.1 81.6 1.0 CE1 C:HIS355 3.4 77.8 1.0 OD1 C:ASP310 3.5 72.2 1.0 NE2 C:HIS179 3.7 56.2 1.0 ND1 C:HIS184 4.1 71.0 1.0 CE1 C:HIS179 4.1 54.0 1.0 CG C:HIS184 4.1 66.4 1.0 CG C:HIS355 4.2 74.3 1.0 CB C:ASP183 4.3 66.0 1.0 ND1 C:HIS355 4.4 79.5 1.0 CB C:ASP310 4.4 65.0 1.0 OE2 C:GLU291 4.5 70.5 1.0 CB C:ALA133 4.6 70.7 1.0 ND1 C:HIS181 4.7 62.8 1.0 CB C:HIS181 4.8 58.0 1.0 CD2 C:HIS179 4.9 57.7 1.0 O C:GLN354 5.0 62.5 1.0

Zinc binding site 6 out of 12 in the Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn701 b:50.2 occ:1.00 OE2 C:GLU291 2.1 70.5 1.0 ND1 C:HIS181 2.2 62.8 1.0 NE2 C:HIS179 2.2 56.2 1.0 OD2 C:ASP310 2.5 76.5 1.0 OE1 C:GLU291 2.6 53.1 1.0 CD C:GLU291 2.7 63.7 1.0 CD2 C:HIS179 2.9 57.7 1.0 CE1 C:HIS181 3.0 65.5 1.0 ZN C:ZN700 3.1 68.5 1.0 CG C:HIS181 3.2 61.7 1.0 CE1 C:HIS179 3.3 54.0 1.0 CG C:ASP310 3.3 70.7 1.0 CB C:HIS181 3.5 58.0 1.0 CB C:ASP310 3.6 65.0 1.0 NE2 C:HIS184 3.8 70.5 1.0 CG C:HIS179 4.0 58.1 1.0 CD2 C:HIS184 4.1 69.5 1.0 NE2 C:HIS181 4.2 67.4 1.0 ND1 C:HIS179 4.2 58.8 1.0 CG C:GLU291 4.2 60.5 1.0 CD2 C:HIS181 4.3 65.0 1.0 OD1 C:ASP183 4.3 81.6 1.0 OD1 C:ASP310 4.4 72.2 1.0 NE2 C:HIS317 4.6 55.6 1.0 O2 C:SO4801 4.7 64.9 1.0 O C:HOH2011 4.7 44.8 1.0 O1 C:SO4801 4.7 87.1 1.0 OD2 C:ASP183 4.7 79.3 1.0 CE1 C:HIS184 4.9 71.6 1.0 CA C:HIS181 5.0 55.0 1.0 CG C:ASP183 5.0 74.9 1.0

Zinc binding site 7 out of 12 in the Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn700 b:85.2 occ:1.00 NE2 D:HIS184 2.0 78.1 1.0 NE2 D:HIS355 2.1 91.1 1.0 OD2 D:ASP310 2.1 0.7 1.0 OD2 D:ASP183 2.2 0.1 1.0 CD2 D:HIS184 2.8 77.5 1.0 CD2 D:HIS355 2.9 88.2 1.0 CG D:ASP310 3.1 99.4 1.0 CE1 D:HIS184 3.1 74.8 1.0 CG D:ASP183 3.1 0.5 1.0 ZN D:ZN701 3.2 80.5 1.0 CE1 D:HIS355 3.2 91.4 1.0 OD1 D:ASP183 3.3 0.3 1.0 OD1 D:ASP310 3.3 0.4 1.0 NE2 D:HIS179 3.5 93.3 1.0 CG D:HIS184 4.1 78.5 1.0 CE1 D:HIS179 4.1 91.9 1.0 CG D:HIS355 4.1 87.7 1.0 ND1 D:HIS184 4.1 73.8 1.0 ND1 D:HIS355 4.2 86.2 1.0 CB D:ASP310 4.4 90.7 1.0 CB D:ASP183 4.5 92.2 1.0 CD2 D:HIS179 4.7 96.7 1.0 OE2 D:GLU291 4.7 90.4 1.0 ND1 D:HIS181 4.9 83.1 1.0 CB D:ALA133 4.9 76.7 1.0 CB D:HIS181 5.0 85.3 1.0

Zinc binding site 8 out of 12 in the Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn701 b:80.5 occ:1.00 OE2 D:GLU291 2.0 90.4 1.0 ND1 D:HIS181 2.2 83.1 1.0 NE2 D:HIS179 2.2 93.3 1.0 OD2 D:ASP310 2.4 0.7 1.0 CD2 D:HIS179 2.6 96.7 1.0 CD D:GLU291 2.8 94.2 1.0 OE1 D:GLU291 3.0 96.9 1.0 CE1 D:HIS181 3.1 85.8 1.0 ZN D:ZN700 3.2 85.2 1.0 CG D:HIS181 3.2 80.9 1.0 CG D:ASP310 3.3 99.4 1.0 CE1 D:HIS179 3.4 91.9 1.0 CB D:HIS181 3.5 85.3 1.0 CB D:ASP310 3.7 90.7 1.0 CG D:HIS179 3.9 99.5 1.0 NE2 D:HIS184 4.0 78.1 1.0 CD2 D:HIS184 4.1 77.5 1.0 CG D:GLU291 4.2 93.0 1.0 ND1 D:HIS179 4.3 99.1 1.0 NE2 D:HIS181 4.3 83.5 1.0 CD2 D:HIS181 4.3 80.0 1.0 OD1 D:ASP183 4.3 0.3 1.0 OD1 D:ASP310 4.4 0.4 1.0 NE2 D:HIS317 4.8 59.9 1.0 OD2 D:ASP183 4.8 0.1 1.0 O1 D:SO4801 5.0 81.5 1.0

Zinc binding site 9 out of 12 in the Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1 within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn700 b:73.2 occ:1.00 NE2 E:HIS184 2.0 81.2 1.0 OD2 E:ASP310 2.0 0.0 1.0 NE2 E:HIS355 2.1 53.6 1.0 OD2 E:ASP183 2.2 96.7 1.0 CD2 E:HIS355 2.9 61.9 1.0 CD2 E:HIS184 3.0 81.8 1.0 CE1 E:HIS184 3.0 81.5 1.0 CG E:ASP310 3.1 93.8 1.0 ZN E:ZN701 3.1 68.7 1.0 CG E:ASP183 3.1 91.1 1.0 CE1 E:HIS355 3.3 61.3 1.0 OD1 E:ASP310 3.4 100.0 1.0 OD1 E:ASP183 3.5 98.5 1.0 NE2 E:HIS179 3.7 64.7 1.0 CE1 E:HIS179 4.0 65.3 1.0 ND1 E:HIS184 4.1 83.4 1.0 CG E:HIS184 4.1 81.5 1.0 CG E:HIS355 4.2 65.0 1.0 ND1 E:HIS355 4.3 62.6 1.0 CB E:ASP310 4.4 89.2 1.0 CB E:ASP183 4.4 78.2 1.0 OE2 E:GLU291 4.5 97.0 1.0 CB E:ALA133 4.7 60.1 1.0 O E:GLN354 4.8 76.6 1.0 ND1 E:HIS181 4.9 65.5 1.0 CD2 E:HIS179 4.9 64.6 1.0 CB E:HIS181 5.0 70.0 1.0

Zinc binding site 10 out of 12 in the Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Structure Determination of the Double Mutant S233Y F250G From the Sec-Alkyl Sulfatase PISA1 within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn701 b:68.7 occ:1.00 OE2 E:GLU291 2.0 97.0 1.0 NE2 E:HIS179 2.0 64.7 1.0 OD2 E:ASP310 2.3 0.0 1.0 ND1 E:HIS181 2.4 65.5 1.0 CD2 E:HIS179 2.8 64.6 1.0 CD E:GLU291 2.9 91.0 1.0 ZN E:ZN700 3.1 73.2 1.0 OE1 E:GLU291 3.1 86.8 1.0 CE1 E:HIS179 3.2 65.3 1.0 CG E:ASP310 3.3 93.8 1.0 CE1 E:HIS181 3.3 69.7 1.0 CG E:HIS181 3.4 65.8 1.0 CB E:HIS181 3.7 70.0 1.0 CB E:ASP310 3.7 89.2 1.0 NE2 E:HIS184 3.8 81.2 1.0 CD2 E:HIS184 4.0 81.8 1.0 CG E:HIS179 4.0 68.6 1.0 ND1 E:HIS179 4.2 67.1 1.0 CG E:GLU291 4.3 88.4 1.0 OD1 E:ASP310 4.3 100.0 1.0 OD1 E:ASP183 4.4 98.5 1.0 NE2 E:HIS181 4.4 75.6 1.0 OD2 E:ASP183 4.5 96.7 1.0 CD2 E:HIS181 4.5 67.6 1.0 NE2 E:HIS317 4.7 63.0 1.0 O E:HOH2010 4.7 48.5 1.0 O2 E:SO4801 4.7 75.8 1.0 O1 E:SO4801 4.8 74.4 1.0 CG E:ASP183 4.9 91.1 1.0 NE2 E:HIS355 4.9 53.6 1.0 CE1 E:HIS184 5.0 81.5 1.0

T.Knaus, M.Schober, B.Kepplinger, M.Faccinelli, J.Pitzer, K.Faber, P.Macheroux, U.Wagner. Structure and Mechanism of An Inverting Alkylsulfatase From Pseudomonas Sp. DSM6611 Specific For Secondary Alkylsulfates. Febs J. V. 279 4374 2012.
ISSN: ISSN 1742-464X
PubMed: 23061549
DOI: 10.1111/FEBS.12027