Fluorine in PDB 7m5x: Human ATP13A2 in the Outward-Facing E2 State Bound to Spermine and Beryllium Fluoride

The structure of Human ATP13A2 in the Outward-Facing E2 State Bound to Spermine and Beryllium Fluoride also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Fluorine atom in the Human ATP13A2 in the Outward-Facing E2 State Bound to Spermine and Beryllium Fluoride (pdb code 7m5x). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Human ATP13A2 in the Outward-Facing E2 State Bound to Spermine and Beryllium Fluoride, PDB code: 7m5x:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Human ATP13A2 in the Outward-Facing E2 State Bound to Spermine and Beryllium Fluoride


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human ATP13A2 in the Outward-Facing E2 State Bound to Spermine and Beryllium Fluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:F1202 b:67.3 occ:1.00 F1 A:BEF1202 0.0 67.3 1.0 BE A:BEF1202 1.5 67.3 1.0 HG1 A:THR750 1.8 64.1 1.0 F3 A:BEF1202 2.5 67.3 1.0 OG1 A:THR750 2.5 64.1 1.0 F2 A:BEF1202 2.6 67.3 1.0 H A:THR515 2.6 66.4 1.0 HA A:THR750 2.6 64.1 1.0 H A:GLY751 2.8 64.5 1.0 HB3 A:LYS514 2.8 64.6 1.0 H A:LYS514 2.9 64.6 1.0 OD1 A:ASP513 3.2 64.3 1.0 CA A:THR750 3.3 64.1 1.0 CB A:THR750 3.3 64.1 1.0 N A:GLY751 3.4 64.5 1.0 H A:ASP752 3.4 64.9 1.0 HB A:THR750 3.4 64.1 1.0 N A:THR515 3.4 66.4 1.0 CB A:LYS514 3.6 64.6 1.0 N A:LYS514 3.6 64.6 1.0 HB2 A:ASP752 3.7 64.9 1.0 HB A:THR515 3.7 66.4 1.0 OG1 A:THR515 3.7 66.4 1.0 HE3 A:LYS514 3.8 64.6 1.0 C A:THR750 3.8 64.1 1.0 OE2 A:GLU348 3.8 68.1 1.0 HB2 A:LYS514 3.8 64.6 1.0 CG A:ASP513 3.9 64.3 1.0 HG1 A:THR515 3.9 66.4 1.0 CA A:LYS514 4.0 64.6 1.0 N A:ASP752 4.1 64.9 1.0 CB A:THR515 4.1 66.4 1.0 OD2 A:ASP513 4.1 64.3 1.0 HZ2 A:LYS859 4.1 66.1 1.0 C A:LYS514 4.2 64.6 1.0 O A:THR346 4.3 65.3 1.0 CA A:THR515 4.4 66.4 1.0 HA3 A:GLY347 4.4 66.3 1.0 CA A:GLY751 4.4 64.5 1.0 HZ3 A:LYS514 4.5 64.6 1.0 CB A:ASP752 4.5 64.9 1.0 HD22 A:ASN881 4.6 67.0 1.0 N A:THR750 4.6 64.1 1.0 HA3 A:GLY751 4.6 64.5 1.0 HA A:ASP513 4.6 64.3 1.0 CG2 A:THR750 4.6 64.1 1.0 CE A:LYS514 4.6 64.6 1.0 C A:GLY751 4.7 64.5 1.0 CD A:GLU348 4.7 68.1 1.0 C A:ASP513 4.8 64.3 1.0 HG23 A:THR750 4.8 64.1 1.0 HB3 A:ASP752 4.8 64.9 1.0 CG A:LYS514 4.8 64.6 1.0 O A:VAL749 4.9 63.5 1.0 CA A:ASP752 4.9 64.9 1.0 O A:THR750 4.9 64.1 1.0 NZ A:LYS859 4.9 66.1 1.0 HA A:LYS514 5.0 64.6 1.0 NZ A:LYS514 5.0 64.6 1.0 HG21 A:THR750 5.0 64.1 1.0 HZ1 A:LYS859 5.0 66.1 1.0

Fluorine binding site 2 out of 3 in the Human ATP13A2 in the Outward-Facing E2 State Bound to Spermine and Beryllium Fluoride


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human ATP13A2 in the Outward-Facing E2 State Bound to Spermine and Beryllium Fluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:F1202 b:67.3 occ:1.00 F2 A:BEF1202 0.0 67.3 1.0 BE A:BEF1202 1.6 67.3 1.0 HB A:THR515 2.1 66.4 1.0 F3 A:BEF1202 2.5 67.3 1.0 F1 A:BEF1202 2.6 67.3 1.0 H A:THR515 2.7 66.4 1.0 OD2 A:ASP513 2.7 64.3 1.0 HA3 A:GLY347 2.9 66.3 1.0 MG A:MG1201 2.9 66.3 1.0 CB A:THR515 3.0 66.4 1.0 OD1 A:ASP513 3.0 64.3 1.0 CG A:ASP513 3.2 64.3 1.0 O A:THR515 3.2 66.4 1.0 N A:THR515 3.3 66.4 1.0 CA A:THR515 3.5 66.4 1.0 OG1 A:THR515 3.5 66.4 1.0 O A:GLY347 3.6 66.3 1.0 HG1 A:THR515 3.6 66.4 1.0 CA A:GLY347 3.7 66.3 1.0 C A:THR515 3.8 66.4 1.0 HD22 A:ASN881 3.9 67.0 1.0 C A:GLY347 3.9 66.3 1.0 O A:HOH1301 3.9 30.0 1.0 H A:LYS514 4.0 64.6 1.0 HA2 A:GLY347 4.0 66.3 1.0 CG2 A:THR515 4.1 66.4 1.0 HG22 A:THR515 4.2 66.4 1.0 O A:THR346 4.2 65.3 1.0 H A:GLY751 4.3 64.5 1.0 HG1 A:THR750 4.3 64.1 1.0 HG21 A:THR515 4.4 66.4 1.0 C A:LYS514 4.4 64.6 1.0 HA A:THR515 4.4 66.4 1.0 N A:LYS514 4.5 64.6 1.0 HB3 A:LYS514 4.5 64.6 1.0 OE2 A:GLU348 4.6 68.1 1.0 ND2 A:ASN881 4.6 67.0 1.0 HA A:THR750 4.7 64.1 1.0 HZ2 A:LYS859 4.7 66.1 1.0 CB A:ASP513 4.7 64.3 1.0 N A:GLY347 4.8 66.3 1.0 OD1 A:ASP878 4.8 68.0 1.0 N A:GLU348 4.9 68.1 1.0 HG23 A:THR515 4.9 66.4 1.0 CA A:LYS514 4.9 64.6 1.0 HG3 A:GLU348 4.9 68.1 1.0 C A:THR346 5.0 65.3 1.0 CD A:GLU348 5.0 68.1 1.0

Fluorine binding site 3 out of 3 in the Human ATP13A2 in the Outward-Facing E2 State Bound to Spermine and Beryllium Fluoride


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Human ATP13A2 in the Outward-Facing E2 State Bound to Spermine and Beryllium Fluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:F1202 b:67.3 occ:1.00 F3 A:BEF1202 0.0 67.3 1.0 BE A:BEF1202 1.5 67.3 1.0 HD22 A:ASN881 2.1 67.0 1.0 H A:GLY751 2.3 64.5 1.0 OD1 A:ASP513 2.4 64.3 1.0 HZ2 A:LYS859 2.4 66.1 1.0 F2 A:BEF1202 2.5 67.3 1.0 F1 A:BEF1202 2.5 67.3 1.0 ND2 A:ASN881 2.8 67.0 1.0 HA3 A:GLY347 3.0 66.3 1.0 HD21 A:ASN881 3.1 67.0 1.0 O A:THR346 3.2 65.3 1.0 HA A:THR750 3.2 64.1 1.0 NZ A:LYS859 3.2 66.1 1.0 N A:GLY751 3.2 64.5 1.0 HZ3 A:LYS859 3.3 66.1 1.0 CG A:ASP513 3.4 64.3 1.0 HZ1 A:LYS859 3.6 66.1 1.0 OD2 A:ASP513 3.7 64.3 1.0 HA3 A:GLY751 3.8 64.5 1.0 C A:THR750 3.9 64.1 1.0 CA A:GLY347 3.9 66.3 1.0 CG A:ASN881 4.0 67.0 1.0 CA A:THR750 4.0 64.1 1.0 HG1 A:THR750 4.0 64.1 1.0 C A:THR346 4.0 65.3 1.0 O A:HOH1301 4.0 30.0 1.0 CA A:GLY751 4.1 64.5 1.0 H A:LYS514 4.2 64.6 1.0 HE3 A:LYS859 4.2 66.1 1.0 OD1 A:ASN881 4.3 67.0 1.0 CE A:LYS859 4.3 66.1 1.0 H A:THR515 4.3 66.4 1.0 N A:GLY347 4.4 66.3 1.0 HA2 A:GLY347 4.4 66.3 1.0 HE2 A:LYS859 4.5 66.1 1.0 HB A:THR515 4.5 66.4 1.0 OG1 A:THR750 4.6 64.1 1.0 MG A:MG1201 4.6 66.3 1.0 H A:ASP752 4.6 64.9 1.0 O A:VAL749 4.7 63.5 1.0 CB A:ASP513 4.7 64.3 1.0 OE2 A:GLU348 4.8 68.1 1.0 C A:GLY347 4.8 66.3 1.0 HA2 A:GLY751 4.8 64.5 1.0 HA A:ASP513 4.8 64.3 1.0 CB A:THR750 4.8 64.1 1.0 HB2 A:ASP513 4.9 64.3 1.0 C A:GLY751 5.0 64.5 1.0 N A:LYS514 5.0 64.6 1.0 N A:THR750 5.0 64.1 1.0 O A:THR750 5.0 64.1 1.0

J.Tillinghast, S.Drury, D.Bowser, A.Benn, K.P.K.Lee. Structural Mechanisms For Gating and Ion Selectivity of the Human Polyamine Transporter ATP13A2. Mol.Cell V. 81 4650 2021.
ISSN: ISSN 1097-2765
PubMed: 34715014
DOI: 10.1016/J.MOLCEL.2021.10.002