Fluorine in PDB 4bbj: Atpase Crystal Structure

The structure of Atpase Crystal Structure, PDB code: 4bbj was solved by D.Mattle, P.Gourdon, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.172 / 2.75
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	242.010, 71.370, 72.430, 90.00, 100.01, 90.00
R / Rfree (%)	19.87 / 24.68

The structure of Atpase Crystal Structure also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Fluorine atom in the Atpase Crystal Structure (pdb code 4bbj). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Atpase Crystal Structure, PDB code: 4bbj:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Atpase Crystal Structure


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Atpase Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:F426 b:57.0 occ:1.00 F1 A:BFD426 0.0 57.0 1.0 BE A:BFD426 1.4 63.2 1.0 OD1 A:BFD426 2.2 69.8 1.0 F3 A:BFD426 2.3 59.5 1.0 F2 A:BFD426 2.3 52.7 1.0 N A:GLY578 2.8 33.4 1.0 ND2 A:ASN627 3.0 52.1 1.0 NZ A:LYS605 3.2 50.5 1.0 OG1 A:THR577 3.2 48.6 1.0 CA A:THR577 3.5 48.1 1.0 CG A:BFD426 3.6 55.9 1.0 C A:THR577 3.6 39.0 1.0 CA A:GLY278 3.6 43.8 1.0 CA A:GLY578 3.8 50.9 1.0 CB A:THR577 3.9 48.0 1.0 CE A:LYS605 4.0 52.4 1.0 O A:HOH2030 4.0 50.0 1.0 OD2 A:BFD426 4.1 52.7 1.0 CG A:ASN627 4.1 54.8 1.0 MG A:MG750 4.2 54.4 1.0 N A:GLY278 4.3 44.4 1.0 O A:LEU576 4.4 69.1 1.0 N A:ASP579 4.5 42.2 1.0 OD1 A:ASN627 4.5 53.0 1.0 C A:GLY578 4.7 47.4 1.0 N A:LYS427 4.7 61.4 1.0 CB A:BFD426 4.7 46.9 1.0 O A:THR277 4.7 50.2 1.0 N A:THR577 4.7 55.5 1.0 C A:GLY278 4.7 50.7 1.0 OD1 A:ASP628 4.8 66.4 1.0 C A:THR277 4.8 46.7 1.0 O A:THR577 4.8 39.7 1.0 O A:GLY278 4.8 57.9 1.0 N A:THR428 4.9 46.9 1.0 OD2 A:ASP628 5.0 81.2 1.0

Fluorine binding site 2 out of 3 in the Atpase Crystal Structure


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Atpase Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:F426 b:52.7 occ:1.00 F2 A:BFD426 0.0 52.7 1.0 BE A:BFD426 1.4 63.2 1.0 MG A:MG750 2.1 54.4 1.0 F3 A:BFD426 2.2 59.5 1.0 OD1 A:BFD426 2.3 69.8 1.0 F1 A:BFD426 2.3 57.0 1.0 OD2 A:BFD426 2.6 52.7 1.0 O A:HOH2030 2.7 50.0 1.0 CG A:BFD426 2.8 55.9 1.0 O A:THR428 3.1 40.9 1.0 O A:HOH2016 3.3 54.7 1.0 CB A:THR428 3.5 40.3 1.0 CA A:GLY278 3.5 43.8 1.0 N A:THR428 3.7 46.9 1.0 CA A:THR428 3.9 46.3 1.0 C A:THR428 3.9 41.8 1.0 ND2 A:ASN627 4.0 52.1 1.0 OD1 A:ASP624 4.1 62.0 1.0 OG1 A:THR428 4.2 42.8 1.0 CB A:BFD426 4.3 46.9 1.0 OD1 A:ASN627 4.4 53.0 1.0 O A:SER274 4.4 45.5 1.0 OG1 A:THR577 4.4 48.6 1.0 N A:GLY278 4.4 44.4 1.0 OD2 A:ASP628 4.5 81.2 1.0 N A:LYS427 4.5 61.4 1.0 CG2 A:THR428 4.5 39.7 1.0 C A:GLY278 4.5 50.7 1.0 O A:GLY278 4.5 57.9 1.0 C A:LYS427 4.6 49.7 1.0 CG A:ASN627 4.6 54.8 1.0 NZ A:LYS605 4.9 50.5 1.0 N A:GLY578 5.0 33.4 1.0

Fluorine binding site 3 out of 3 in the Atpase Crystal Structure


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Atpase Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:F426 b:59.5 occ:1.00 F3 A:BFD426 0.0 59.5 1.0 BE A:BFD426 1.4 63.2 1.0 F2 A:BFD426 2.2 52.7 1.0 F1 A:BFD426 2.3 57.0 1.0 OD1 A:BFD426 2.3 69.8 1.0 OG1 A:THR577 2.5 48.6 1.0 N A:THR428 2.7 46.9 1.0 N A:LYS427 3.0 61.4 1.0 CG A:BFD426 3.1 55.9 1.0 OD2 A:BFD426 3.4 52.7 1.0 CB A:THR577 3.4 48.0 1.0 CA A:LYS427 3.5 53.4 1.0 C A:LYS427 3.5 49.7 1.0 CB A:LYS427 3.5 39.8 1.0 CB A:THR428 3.5 40.3 1.0 OG1 A:THR428 3.6 42.8 1.0 CA A:THR428 3.6 46.3 1.0 CA A:THR577 3.8 48.1 1.0 MG A:MG750 4.0 54.4 1.0 C A:BFD426 4.0 52.4 1.0 O A:THR428 4.0 40.9 1.0 N A:GLY578 4.1 33.4 1.0 CB A:BFD426 4.2 46.9 1.0 CA A:GLY278 4.3 43.8 1.0 C A:THR428 4.3 41.8 1.0 CA A:BFD426 4.4 47.6 1.0 O A:GLY278 4.4 57.9 1.0 C A:THR577 4.5 39.0 1.0 O A:LEU576 4.5 69.1 1.0 NZ A:LYS605 4.6 50.5 1.0 O A:LYS427 4.6 51.4 1.0 CG A:LYS427 4.7 42.4 1.0 O A:HOH2030 4.7 50.0 1.0 CE A:LYS427 4.7 51.6 1.0 CG2 A:THR577 4.7 35.2 1.0 N A:ASP579 4.8 42.2 1.0 C A:GLY278 4.9 50.7 1.0 CG2 A:THR428 5.0 39.7 1.0 N A:THR577 5.0 55.5 1.0

M.Andersson, D.Mattle, O.Sitsel, T.Klymchuk, A.Nielsen, L.B.Moller, S.H.White, P.Nissen, P.Gourdon. Copper-Transporting P-Type Atpases Use A Unique Ion-Release Pathway Nat.Struct.Mol.Biol. V. 21 43 2014.
ISSN: ISSN 1545-9993
PubMed: 24317491
DOI: 10.1038/NSMB.2721