Fluorine in PDB 4umv: Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State

All present enzymatic activity of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State:
3.6.3.5;

The structure of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State, PDB code: 4umv was solved by K.T.Wang, O.Sitsel, G.Meloni, H.E.Autzen, M.Andersson, T.Klymchuk, A.M.Nielsen, D.C.Rees, P.Nissen, P.Gourdon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.082 / 3.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	54.462, 60.972, 141.523, 90.00, 95.99, 90.00
R / Rfree (%)	21.85 / 28.14

The structure of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State (pdb code 4umv). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State, PDB code: 4umv:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State within 5.0Å range: probe atom residue distance (Å) B Occ A:F1732 b:64.7 occ:1.00 F1 A:BEF1732 0.0 64.7 1.0 BE A:BEF1732 1.5 75.8 1.0 MG A:MG1731 1.9 71.2 1.0 O A:THR438 2.5 41.6 1.0 OD2 A:ASP436 2.5 30.4 1.0 F3 A:BEF1732 2.5 74.2 1.0 F2 A:BEF1732 2.5 96.1 1.0 OD1 A:ASP628 2.9 43.5 1.0 OD2 A:ASP628 3.0 51.2 1.0 CB A:THR438 3.1 27.7 1.0 CG A:ASP436 3.2 33.6 1.0 C A:THR438 3.3 35.1 1.0 CG A:ASP628 3.4 49.8 1.0 OD1 A:ASP436 3.4 38.0 1.0 CA A:THR438 3.5 29.9 1.0 N A:THR438 3.5 32.4 1.0 OG1 A:THR438 3.6 31.3 1.0 CA A:GLY289 3.7 34.1 1.0 CG2 A:THR438 4.3 24.6 1.0 O A:GLY289 4.3 34.8 1.0 O A:SER285 4.4 32.5 1.0 C A:LYS437 4.4 35.0 1.0 C A:GLY289 4.5 48.6 1.0 N A:GLY439 4.6 34.6 1.0 CB A:ASP436 4.6 34.0 1.0 OD2 A:ASP632 4.7 51.9 1.0 N A:GLY289 4.8 33.6 1.0 N A:LYS437 4.8 35.2 1.0 CG2 A:THR440 4.9 26.1 1.0 OD1 A:ASN631 4.9 35.8 1.0 CB A:ASP628 4.9 50.1 1.0 O A:LYS437 4.9 38.3 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State within 5.0Å range: probe atom residue distance (Å) B Occ A:F1732 b:96.1 occ:1.00 F2 A:BEF1732 0.0 96.1 1.0 BE A:BEF1732 1.5 75.8 1.0 F1 A:BEF1732 2.5 64.7 1.0 F3 A:BEF1732 2.6 74.2 1.0 OD1 A:ASN631 2.7 35.8 1.0 ND2 A:ASN631 2.8 42.8 1.0 OD2 A:ASP436 3.0 30.4 1.0 CA A:GLY289 3.0 34.1 1.0 CG A:ASN631 3.1 40.5 1.0 MG A:MG1731 3.2 71.2 1.0 N A:GLY289 3.5 33.6 1.0 O A:SER285 3.7 32.5 1.0 CG A:ASP436 3.9 33.6 1.0 NZ A:LYS610 4.1 29.5 1.0 OD1 A:ASP436 4.2 38.0 1.0 OD1 A:ASP628 4.2 43.5 1.0 OD2 A:ASP632 4.2 51.9 1.0 C A:THR288 4.3 34.1 1.0 OD2 A:ASP628 4.4 51.2 1.0 C A:GLY289 4.4 48.6 1.0 OD1 A:ASP632 4.5 50.0 1.0 O A:THR288 4.6 35.0 1.0 CB A:ASN631 4.6 42.6 1.0 CG A:ASP628 4.7 49.8 1.0 CG A:ASP632 4.7 51.7 1.0 O A:GLY289 4.8 34.8 1.0 O A:THR438 4.9 41.6 1.0 C A:SER285 4.9 38.5 1.0 CE A:LYS610 5.0 34.3 1.0 O A:LEU287 5.0 49.5 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State within 5.0Å range: probe atom residue distance (Å) B Occ A:F1732 b:74.2 occ:1.00 F3 A:BEF1732 0.0 74.2 1.0 BE A:BEF1732 1.6 75.8 1.0 OD1 A:ASP436 2.4 38.0 1.0 F1 A:BEF1732 2.5 64.7 1.0 F2 A:BEF1732 2.6 96.1 1.0 OD2 A:ASP436 2.9 30.4 1.0 CG A:ASP436 2.9 33.6 1.0 CA A:GLY289 3.1 34.1 1.0 OG1 A:THR583 3.2 44.3 1.0 O A:GLY289 3.6 34.8 1.0 OG1 A:THR438 3.6 31.3 1.0 N A:GLY584 3.7 31.7 1.0 NZ A:LYS610 3.8 29.5 1.0 C A:GLY289 3.8 48.6 1.0 CB A:THR583 4.0 41.4 1.0 CA A:THR583 4.0 36.3 1.0 CB A:THR438 4.0 27.7 1.0 N A:THR438 4.1 32.4 1.0 MG A:MG1731 4.2 71.2 1.0 N A:GLY289 4.3 33.6 1.0 CB A:ASP436 4.4 34.0 1.0 C A:THR583 4.4 39.8 1.0 N A:LYS437 4.4 35.2 1.0 CA A:THR438 4.6 29.9 1.0 O A:THR288 4.6 35.0 1.0 ND2 A:ASN631 4.6 42.8 1.0 N A:ASP585 4.7 34.4 1.0 CA A:GLY584 4.7 26.8 1.0 O A:THR438 4.7 41.6 1.0 OD1 A:ASN631 4.8 35.8 1.0 CG A:LYS437 4.8 40.6 1.0 CE A:LYS610 4.8 34.3 1.0 O A:LEU582 4.8 31.4 1.0 OD1 A:ASP628 4.9 43.5 1.0 C A:THR288 4.9 34.1 1.0 C A:LYS437 5.0 35.0 1.0

K.Wang, O.Sitsel, G.Meloni, H.E.Autzen, M.Andersson, T.Klymchuk, A.M.Nielsen, D.C.Rees, P.Nissen, P.Gourdon. Structure and Mechanism of Zn(2+)-Transporting P-Type Atpases. Nature V. 514 518 2014.
ISSN: ESSN 0028-0836
PubMed: 25132545
DOI: 10.1038/NATURE13618