Fluorine in PDB 7u1y: Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+

The structure of Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+, PDB code: 7u1y was solved by A.Jacewicz, A.M.Sanchez, S.Shuman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.28 / 1.81
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	133.721, 133.721, 56.69, 90, 90, 90
R / Rfree (%)	15.6 / 18.2

The structure of Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+ also contains other interesting chemical elements:

Potassium	(K)	1 atom
Aluminium	(Al)	1 atom
Cobalt	(Co)	2 atoms

The binding sites of Fluorine atom in the Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+ (pdb code 7u1y). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+, PDB code: 7u1y:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:20.1 occ:1.00 F1 A:ALF501 0.0 20.1 1.0 AL A:ALF501 1.8 17.8 1.0 CO A:CO502 1.9 14.4 0.7 F4 A:ALF501 2.5 21.3 1.0 O A:HOH854 2.5 20.9 1.0 F3 A:ALF501 2.6 18.3 1.0 OD2 A:ASP248 2.6 15.3 1.0 O A:HOH759 2.7 18.0 1.0 O A:HOH688 2.8 17.1 1.0 OD1 A:ASP248 2.8 13.9 1.0 CG A:ASP248 3.1 17.8 1.0 OD1 A:ASN249 3.1 16.4 1.0 ND2 A:ASN249 3.3 13.3 1.0 CG A:ASP195 3.3 23.9 1.0 O A:HOH957 3.4 23.8 1.0 OD2 A:ASP195 3.4 26.2 1.0 F2 A:ALF501 3.5 19.3 1.0 CG A:ASN249 3.6 19.0 1.0 OD1 A:ASP195 3.6 25.2 1.0 O A:HOH758 3.6 33.8 0.6 CB A:ASP195 3.8 22.2 1.0 OD1 A:ASP286 3.9 17.6 1.0 CA A:ASP195 4.5 22.6 1.0 CB A:ASP248 4.6 16.8 1.0 O A:HOH724 4.7 16.4 1.0 CG A:ASP286 4.9 16.6 1.0 OD2 A:ASP286 5.0 18.0 1.0

Fluorine binding site 2 out of 4 in the Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:19.3 occ:1.00 F2 A:ALF501 0.0 19.3 1.0 AL A:ALF501 1.8 17.8 1.0 F4 A:ALF501 2.5 21.3 1.0 O A:HOH854 2.5 20.9 1.0 N A:ASP363 2.5 17.4 1.0 F3 A:ALF501 2.6 18.3 1.0 OD2 A:ASP248 2.6 15.3 1.0 NZ A:LYS401 2.9 20.1 1.0 CA A:GLY362 3.0 14.7 1.0 OD2 A:ASP363 3.0 25.5 1.0 ND2 A:ASN192 3.1 21.0 1.0 OD1 A:ASN192 3.2 23.1 1.0 C A:GLY362 3.2 17.0 1.0 CG A:ASN192 3.5 23.2 1.0 F1 A:ALF501 3.5 20.1 1.0 CG A:ASP363 3.6 27.2 1.0 CA A:ASP363 3.6 19.2 1.0 CB A:ASP363 3.6 21.1 1.0 CE A:LYS401 3.7 21.8 1.0 CG A:ASP248 3.9 17.8 1.0 O A:HOH724 4.2 16.4 1.0 O A:ASN192 4.3 21.3 1.0 N A:GLY362 4.4 16.6 1.0 N A:LEU364 4.4 17.6 1.0 O A:GLY362 4.5 16.7 1.0 C A:ASP363 4.6 18.5 1.0 OD1 A:ASP363 4.6 25.0 1.0 O A:THR399 4.7 23.1 1.0 OD1 A:ASP248 4.7 13.9 1.0 ND2 A:ASN249 4.7 13.3 1.0 CB A:ASP248 4.8 16.8 1.0 CB A:ASN192 5.0 18.0 1.0

Fluorine binding site 3 out of 4 in the Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:18.3 occ:1.00 F3 A:ALF501 0.0 18.3 1.0 AL A:ALF501 1.8 17.8 1.0 O A:HOH854 2.5 20.9 1.0 F1 A:ALF501 2.6 20.1 1.0 OD2 A:ASP248 2.6 15.3 1.0 F2 A:ALF501 2.6 19.3 1.0 O A:HOH724 2.7 16.4 1.0 N A:LEU364 2.9 17.6 1.0 O A:HOH957 3.0 23.8 1.0 O A:HOH759 3.0 18.0 1.0 N A:ASP363 3.1 17.4 1.0 CG A:ASP248 3.2 17.8 1.0 OD1 A:ASP248 3.4 13.9 1.0 F4 A:ALF501 3.6 21.3 1.0 CB A:LEU364 3.7 16.6 1.0 CO A:CO502 3.7 14.4 0.7 CA A:ASP363 3.7 19.2 1.0 C A:ASP363 3.8 18.5 1.0 CB A:ASP363 3.8 21.1 1.0 C A:GLY362 3.8 17.0 1.0 CA A:LEU364 3.9 15.5 1.0 CA A:GLY362 4.1 14.7 1.0 CB A:ASP248 4.4 16.8 1.0 OD2 A:ASP363 4.4 25.5 1.0 O A:HOH758 4.6 33.8 0.6 CG A:ASP363 4.7 27.2 1.0 O A:HOH823 4.7 24.3 1.0 O A:GLY362 4.7 16.7 1.0 O A:HOH814 4.7 15.7 1.0 N A:ASN365 4.8 14.5 1.0 O A:LYS361 4.9 16.5 1.0 C A:LEU364 4.9 17.8 1.0 ND2 A:ASN192 4.9 21.0 1.0 O A:HOH688 4.9 17.1 1.0 O A:ASP363 5.0 18.9 1.0 OD2 A:ASP195 5.0 26.2 1.0

Fluorine binding site 4 out of 4 in the Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structure of SPAC806.04C Protein From Fission Yeast Bound to ALF4 and CO2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:21.3 occ:1.00 F4 A:ALF501 0.0 21.3 1.0 AL A:ALF501 1.8 17.8 1.0 F2 A:ALF501 2.5 19.3 1.0 F1 A:ALF501 2.5 20.1 1.0 OD2 A:ASP248 2.6 15.3 1.0 O A:HOH854 2.7 20.9 1.0 ND2 A:ASN249 2.7 13.3 1.0 CB A:ASP195 3.1 22.2 1.0 NZ A:LYS401 3.2 20.1 1.0 CE A:LYS401 3.3 21.8 1.0 O A:ASN192 3.3 21.3 1.0 ND2 A:ASN192 3.4 21.0 1.0 F3 A:ALF501 3.6 18.3 1.0 CG A:ASP195 3.6 23.9 1.0 CG A:ASP248 3.6 17.8 1.0 OD2 A:ASP195 3.7 26.2 1.0 CG A:ASN249 3.8 19.0 1.0 CA A:ASP195 3.9 22.6 1.0 CO A:CO502 4.1 14.4 0.7 OD1 A:ASN249 4.1 16.4 1.0 CG A:ASN192 4.1 23.2 1.0 OD1 A:ASP248 4.1 13.9 1.0 N A:ASP195 4.3 23.1 1.0 OD1 A:ASN192 4.3 23.1 1.0 OD1 A:ASP195 4.4 25.2 1.0 OD2 A:ASP363 4.4 25.5 1.0 C A:ASN192 4.5 17.4 1.0 OE1 A:GLU253 4.5 21.6 1.0 CD A:LYS401 4.8 29.9 1.0 CB A:ASP248 4.8 16.8 1.0 C A:THR194 4.8 22.4 1.0 O A:HOH688 4.9 17.1 1.0 N A:ASP363 4.9 17.4 1.0 CA A:ASN192 5.0 18.6 1.0

A.M.Sanchez, A.Jacewicz, S.Shuman. Fission Yeast DUF89 and DUF8901 Are Cobalt/Nickel-Dependent Phosphatase-Pyrophosphatases That Act Via A Covalent Aspartyl-Phosphate Intermediate. J.Biol.Chem. V. 298 01851 2022.
ISSN: ESSN 1083-351X
PubMed: 35314193
DOI: 10.1016/J.JBC.2022.101851