Fluorine in PDB 7x0v: Cryo-Em Structure of Human Tric-Adp-Alfx

The structure of Cryo-Em Structure of Human Tric-Adp-Alfx also contains other interesting chemical elements:

Aluminium	(Al)	16 atoms
Magnesium	(Mg)	16 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 40; Page 5, Binding sites: 41 - 48;

Binding sites:

The binding sites of Fluorine atom in the Cryo-Em Structure of Human Tric-Adp-Alfx (pdb code 7x0v). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 48 binding sites of Fluorine where determined in the Cryo-Em Structure of Human Tric-Adp-Alfx, PDB code: 7x0v:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Fluorine binding site 1 out of 48 in the Cryo-Em Structure of Human Tric-Adp-Alfx


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Cryo-Em Structure of Human Tric-Adp-Alfx within 5.0Å range: probe atom residue distance (Å) B Occ K:F603 b:6.1 occ:1.00 F1 K:AF3603 0.0 6.1 1.0 OD1 K:ASP90 1.6 39.0 1.0 AL K:AF3603 1.7 6.1 1.0 MG K:MG602 2.1 4.6 1.0 O2B K:ADP601 2.2 5.0 1.0 CG K:ASP90 2.5 39.0 1.0 NZ K:LYS159 2.6 38.1 1.0 F3 K:AF3603 3.0 6.1 1.0 F2 K:AF3603 3.0 6.1 1.0 O3A K:ADP601 3.0 5.0 1.0 PB K:ADP601 3.2 5.0 1.0 OD2 K:ASP90 3.2 39.0 1.0 OD1 K:ASP393 3.3 41.1 1.0 O2A K:ADP601 3.5 5.0 1.0 OD1 K:ASP59 3.5 43.7 1.0 PA K:ADP601 3.6 5.0 1.0 CB K:ASP90 3.6 39.0 1.0 CA K:ASP90 3.7 39.0 1.0 O1A K:ADP601 3.8 5.0 1.0 OD2 K:ASP393 3.9 41.1 1.0 O3B K:ADP601 3.9 5.0 1.0 CG K:ASP393 3.9 41.1 1.0 CE K:LYS159 4.0 38.1 1.0 N K:GLY91 4.0 38.1 1.0 C K:ASP90 4.4 39.0 1.0 O1B K:ADP601 4.5 5.0 1.0 O K:HOH701 4.6 4.8 1.0 CG K:ASP59 4.7 43.7 1.0 N K:THR92 4.8 37.3 1.0 N K:ASP90 4.8 39.0 1.0 OG1 K:THR158 5.0 39.5 1.0

Fluorine binding site 2 out of 48 in the Cryo-Em Structure of Human Tric-Adp-Alfx


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Cryo-Em Structure of Human Tric-Adp-Alfx within 5.0Å range: probe atom residue distance (Å) B Occ K:F603 b:6.1 occ:1.00 F2 K:AF3603 0.0 6.1 1.0 AL K:AF3603 1.7 6.1 1.0 OD1 K:ASP59 1.8 43.7 1.0 O K:HOH701 2.2 4.8 1.0 CG K:ASP59 2.7 43.7 1.0 OD1 K:ASP393 2.9 41.1 1.0 F3 K:AF3603 3.0 6.1 1.0 F1 K:AF3603 3.0 6.1 1.0 OD2 K:ASP59 3.1 43.7 1.0 NZ K:LYS159 3.4 38.1 1.0 OG1 K:THR92 3.7 37.3 1.0 CE K:LYS159 3.8 38.1 1.0 OD1 K:ASP85 3.8 41.2 1.0 O K:GLY89 3.9 38.4 1.0 OD1 K:ASP90 3.9 39.0 1.0 OD2 K:ASP85 4.0 41.2 1.0 CG K:ASP393 4.0 41.1 1.0 CG K:ASP85 4.0 41.2 1.0 CB K:ASP59 4.1 43.7 1.0 CA K:ASP90 4.1 39.0 1.0 O2B K:ADP601 4.2 5.0 1.0 CB K:THR92 4.3 37.3 1.0 C K:GLY89 4.4 38.4 1.0 N K:ASP90 4.6 39.0 1.0 CG K:ASP90 4.7 39.0 1.0 CB K:ASP393 4.7 41.1 1.0 OD2 K:ASP393 4.8 41.1 1.0 CA K:ASP59 4.8 43.7 1.0 N K:GLY60 4.8 41.5 1.0 MG K:MG602 4.9 4.6 1.0 CB K:ASP90 4.9 39.0 1.0 N K:THR92 5.0 37.3 1.0 C K:ASP90 5.0 39.0 1.0

Fluorine binding site 3 out of 48 in the Cryo-Em Structure of Human Tric-Adp-Alfx


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Cryo-Em Structure of Human Tric-Adp-Alfx within 5.0Å range: probe atom residue distance (Å) B Occ K:F603 b:6.1 occ:1.00 F3 K:AF3603 0.0 6.1 1.0 AL K:AF3603 1.7 6.1 1.0 O2B K:ADP601 2.2 5.0 1.0 CB K:THR92 2.8 37.3 1.0 OD1 K:ASP59 2.9 43.7 1.0 F1 K:AF3603 3.0 6.1 1.0 F2 K:AF3603 3.0 6.1 1.0 N K:THR93 3.0 38.0 1.0 N K:THR92 3.1 37.3 1.0 OG1 K:THR92 3.1 37.3 1.0 CA K:THR92 3.3 37.3 1.0 OG1 K:THR93 3.4 38.0 1.0 PB K:ADP601 3.4 5.0 1.0 N K:GLY60 3.5 41.5 1.0 C K:THR92 3.5 37.3 1.0 O3B K:ADP601 3.7 5.0 1.0 OD1 K:ASP90 3.7 39.0 1.0 CG K:ASP59 3.8 43.7 1.0 CA K:GLY60 4.1 41.5 1.0 CG2 K:THR92 4.1 37.3 1.0 CB K:THR93 4.1 38.0 1.0 CA K:THR93 4.1 38.0 1.0 N K:GLY91 4.3 38.1 1.0 OD2 K:ASP59 4.3 43.7 1.0 C K:GLY91 4.4 38.1 1.0 O1B K:ADP601 4.4 5.0 1.0 O3A K:ADP601 4.5 5.0 1.0 C K:ASP59 4.5 43.7 1.0 NZ K:LYS159 4.5 38.1 1.0 CA K:ASP59 4.6 43.7 1.0 N K:ASN61 4.7 41.9 1.0 MG K:MG602 4.7 4.6 1.0 O K:THR92 4.7 37.3 1.0 CB K:ASP59 4.8 43.7 1.0 C K:GLY60 4.8 41.5 1.0 CA K:GLY91 4.9 38.1 1.0 CG K:ASP90 4.9 39.0 1.0 CA K:ASP90 5.0 39.0 1.0

Fluorine binding site 4 out of 48 in the Cryo-Em Structure of Human Tric-Adp-Alfx


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Cryo-Em Structure of Human Tric-Adp-Alfx within 5.0Å range: probe atom residue distance (Å) B Occ J:F603 b:6.8 occ:1.00 F1 J:AF3603 0.0 6.8 1.0 AL J:AF3603 1.7 6.8 1.0 ND2 J:ASN102 2.2 40.5 1.0 CE J:LYS171 2.4 41.9 1.0 O1A J:ADP601 2.7 6.9 1.0 O2A J:ADP601 2.9 6.9 1.0 F2 J:AF3603 2.9 6.8 1.0 F3 J:AF3603 2.9 6.8 1.0 NZ J:LYS171 3.0 41.9 1.0 CG J:ASN102 3.1 40.5 1.0 PA J:ADP601 3.2 6.9 1.0 O1B J:ADP601 3.3 6.9 1.0 OD1 J:ASP68 3.3 45.8 1.0 OD1 J:ASN102 3.3 40.5 1.0 O2B J:ADP601 3.4 6.9 1.0 MG J:MG602 3.5 9.8 1.0 CD J:LYS171 3.8 41.9 1.0 PB J:ADP601 3.8 6.9 1.0 O3A J:ADP601 4.0 6.9 1.0 CG J:LYS171 4.1 41.9 1.0 CG J:ASP68 4.1 45.8 1.0 CA J:ASP68 4.4 45.8 1.0 OG J:SER170 4.5 41.2 1.0 CB J:ASN102 4.5 40.5 1.0 CB J:ASP68 4.6 45.8 1.0 O5' J:ADP601 4.6 6.9 1.0 OD1 J:ASP99 4.6 39.5 1.0 O J:ASN67 4.7 44.1 1.0 OD2 J:ASP68 5.0 45.8 1.0 CB J:SER170 5.0 41.2 1.0

Fluorine binding site 5 out of 48 in the Cryo-Em Structure of Human Tric-Adp-Alfx


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Cryo-Em Structure of Human Tric-Adp-Alfx within 5.0Å range: probe atom residue distance (Å) B Occ J:F603 b:6.8 occ:1.00 F2 J:AF3603 0.0 6.8 1.0 AL J:AF3603 1.7 6.8 1.0 NZ J:LYS171 1.8 41.9 1.0 O2B J:ADP601 2.8 6.9 1.0 CE J:LYS171 2.9 41.9 1.0 OD1 J:ASP99 2.9 39.5 1.0 F3 J:AF3603 2.9 6.8 1.0 F1 J:AF3603 2.9 6.8 1.0 OD1 J:ASP68 3.0 45.8 1.0 O J:HOH701 3.3 3.5 1.0 CG J:ASP68 3.5 45.8 1.0 OD2 J:ASP394 3.6 44.4 1.0 OD2 J:ASP68 3.6 45.8 1.0 PB J:ADP601 3.9 6.9 1.0 O1B J:ADP601 3.9 6.9 1.0 CG J:ASP394 3.9 44.4 1.0 MG J:MG602 3.9 9.8 1.0 CG J:ASP99 4.0 39.5 1.0 N J:GLY100 4.0 38.5 1.0 OD1 J:ASP394 4.1 44.4 1.0 OD1 J:ASN102 4.2 40.5 1.0 O2A J:ADP601 4.2 6.9 1.0 CA J:ASP99 4.2 39.5 1.0 CD J:LYS171 4.2 41.9 1.0 OG1 J:THR101 4.3 38.9 1.0 ND2 J:ASN102 4.4 40.5 1.0 O J:GLY98 4.6 40.3 1.0 N J:THR101 4.7 38.9 1.0 CB J:ASP99 4.7 39.5 1.0 C J:ASP99 4.7 39.5 1.0 CG J:ASN102 4.7 40.5 1.0 CB J:ASP68 4.7 45.8 1.0 CB J:ASP394 4.8 44.4 1.0 PA J:ADP601 4.9 6.9 1.0 O3A J:ADP601 4.9 6.9 1.0 O3B J:ADP601 4.9 6.9 1.0 OD2 J:ASP99 4.9 39.5 1.0

Fluorine binding site 6 out of 48 in the Cryo-Em Structure of Human Tric-Adp-Alfx


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Cryo-Em Structure of Human Tric-Adp-Alfx within 5.0Å range: probe atom residue distance (Å) B Occ J:F603 b:6.8 occ:1.00 F3 J:AF3603 0.0 6.8 1.0 OD1 J:ASN102 1.3 40.5 1.0 AL J:AF3603 1.7 6.8 1.0 OD1 J:ASP68 2.1 45.8 1.0 O1B J:ADP601 2.2 6.9 1.0 CG J:ASN102 2.3 40.5 1.0 OG1 J:THR101 2.4 38.9 1.0 ND2 J:ASN102 2.8 40.5 1.0 F2 J:AF3603 2.9 6.8 1.0 F1 J:AF3603 2.9 6.8 1.0 N J:ASN102 3.1 40.5 1.0 PB J:ADP601 3.3 6.9 1.0 CG J:ASP68 3.4 45.8 1.0 O2B J:ADP601 3.5 6.9 1.0 CB J:ASN102 3.6 40.5 1.0 N J:THR101 3.6 38.9 1.0 N J:ALA69 3.6 42.5 1.0 CB J:THR101 3.7 38.9 1.0 C J:THR101 3.8 38.9 1.0 CA J:THR101 3.9 38.9 1.0 CA J:ASN102 3.9 40.5 1.0 OD2 J:ASP68 4.1 45.8 1.0 O1A J:ADP601 4.1 6.9 1.0 NZ J:LYS171 4.2 41.9 1.0 CA J:ASP68 4.3 45.8 1.0 N J:ALA70 4.3 43.6 1.0 O3B J:ADP601 4.3 6.9 1.0 CB J:ALA69 4.3 42.5 1.0 CE J:LYS171 4.4 41.9 1.0 C J:ASP68 4.4 45.8 1.0 CB J:ASP68 4.4 45.8 1.0 O3A J:ADP601 4.4 6.9 1.0 CA J:ALA69 4.4 42.5 1.0 CG2 J:THR101 4.5 38.9 1.0 C J:GLY100 4.6 38.5 1.0 PA J:ADP601 4.7 6.9 1.0 N J:GLY100 4.8 38.5 1.0 C J:ALA69 4.8 42.5 1.0 O J:THR101 4.9 38.9 1.0 O2A J:ADP601 4.9 6.9 1.0 CA J:GLY100 5.0 38.5 1.0

Fluorine binding site 7 out of 48 in the Cryo-Em Structure of Human Tric-Adp-Alfx


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of Cryo-Em Structure of Human Tric-Adp-Alfx within 5.0Å range: probe atom residue distance (Å) B Occ H:F603 b:6.8 occ:1.00 F1 H:AF3603 0.0 6.8 1.0 AL H:AF3603 1.7 6.8 1.0 O1A H:ADP601 2.7 6.9 1.0 NZ H:LYS166 2.8 40.4 1.0 O2A H:ADP601 2.9 6.9 1.0 F3 H:AF3603 2.9 6.8 1.0 F2 H:AF3603 2.9 6.8 1.0 PA H:ADP601 3.2 6.9 1.0 O1B H:ADP601 3.3 6.9 1.0 O2B H:ADP601 3.4 6.9 1.0 MG H:MG602 3.5 9.8 1.0 CE H:LYS166 3.6 40.4 1.0 PB H:ADP601 3.8 6.9 1.0 O3A H:ADP601 4.0 6.9 1.0 OG H:SER165 4.0 40.7 1.0 O H:ASP92 4.0 40.4 1.0 OD1 H:ASP61 4.0 41.2 1.0 OG1 H:THR94 4.1 39.0 1.0 OG1 H:THR95 4.3 38.4 1.0 OD2 H:ASP391 4.5 38.9 1.0 CG2 H:THR95 4.6 38.4 1.0 O5' H:ADP601 4.6 6.9 1.0 CA H:ASP61 4.7 41.2 1.0 CD H:LYS166 4.7 40.4 1.0 O H:ASN60 4.8 40.6 1.0 CG H:ASP61 4.8 41.2 1.0

Fluorine binding site 8 out of 48 in the Cryo-Em Structure of Human Tric-Adp-Alfx


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of Cryo-Em Structure of Human Tric-Adp-Alfx within 5.0Å range: probe atom residue distance (Å) B Occ H:F603 b:6.8 occ:1.00 F2 H:AF3603 0.0 6.8 1.0 AL H:AF3603 1.7 6.8 1.0 OD2 H:ASP391 2.5 38.9 1.0 O H:ASP92 2.5 40.4 1.0 O2B H:ADP601 2.8 6.9 1.0 F3 H:AF3603 2.9 6.8 1.0 F1 H:AF3603 2.9 6.8 1.0 OD1 H:ASP61 3.1 41.2 1.0 CA H:ASP92 3.1 40.4 1.0 CG H:ASP391 3.2 38.9 1.0 C H:ASP92 3.2 40.4 1.0 NZ H:LYS166 3.2 40.4 1.0 O H:HOH701 3.5 2.3 1.0 OG1 H:THR94 3.7 39.0 1.0 CG H:ASP61 3.7 41.2 1.0 CB H:ASP391 3.8 38.9 1.0 CB H:ASP92 3.8 40.4 1.0 PB H:ADP601 3.9 6.9 1.0 OD1 H:ASP391 3.9 38.9 1.0 O1B H:ADP601 3.9 6.9 1.0 O H:GLY91 3.9 39.0 1.0 MG H:MG602 3.9 9.8 1.0 OD2 H:ASP61 4.0 41.2 1.0 CE H:LYS166 4.0 40.4 1.0 O2A H:ADP601 4.2 6.9 1.0 N H:ASP92 4.3 40.4 1.0 CG2 H:THR94 4.5 39.0 1.0 N H:GLY93 4.5 39.7 1.0 C H:GLY91 4.5 39.0 1.0 CB H:THR94 4.7 39.0 1.0 CB H:ASP61 4.7 41.2 1.0 N H:THR94 4.9 39.0 1.0 PA H:ADP601 4.9 6.9 1.0 O3A H:ADP601 4.9 6.9 1.0 O3B H:ADP601 4.9 6.9 1.0

Fluorine binding site 9 out of 48 in the Cryo-Em Structure of Human Tric-Adp-Alfx


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 9 of Cryo-Em Structure of Human Tric-Adp-Alfx within 5.0Å range: probe atom residue distance (Å) B Occ H:F603 b:6.8 occ:1.00 F3 H:AF3603 0.0 6.8 1.0 OG1 H:THR94 1.2 39.0 1.0 AL H:AF3603 1.7 6.8 1.0 OD1 H:ASP61 2.0 41.2 1.0 O1B H:ADP601 2.2 6.9 1.0 CB H:THR94 2.6 39.0 1.0 F1 H:AF3603 2.9 6.8 1.0 F2 H:AF3603 2.9 6.8 1.0 CG H:ASP61 3.2 41.2 1.0 N H:GLY62 3.2 40.1 1.0 O H:ASP92 3.2 40.4 1.0 PB H:ADP601 3.3 6.9 1.0 N H:THR95 3.3 38.4 1.0 CG2 H:THR94 3.4 39.0 1.0 O2B H:ADP601 3.5 6.9 1.0 CA H:THR94 3.5 39.0 1.0 N H:THR94 3.6 39.0 1.0 CG2 H:THR95 3.6 38.4 1.0 CA H:ASP61 3.7 41.2 1.0 C H:THR94 3.9 39.0 1.0 C H:ASP61 4.0 41.2 1.0 CB H:ASP61 4.0 41.2 1.0 OD2 H:ASP61 4.1 41.2 1.0 O1A H:ADP601 4.1 6.9 1.0 OG1 H:THR95 4.2 38.4 1.0 CA H:GLY62 4.2 40.1 1.0 CB H:THR95 4.3 38.4 1.0 O3B H:ADP601 4.3 6.9 1.0 C H:ASP92 4.4 40.4 1.0 CA H:THR95 4.4 38.4 1.0 O3A H:ADP601 4.4 6.9 1.0 NZ H:LYS166 4.5 40.4 1.0 PA H:ADP601 4.7 6.9 1.0 C H:GLY93 4.7 39.7 1.0 OD2 H:ASP391 4.7 38.9 1.0 O H:HOH701 4.8 2.3 1.0 O H:ASN60 4.8 40.6 1.0 N H:ALA63 4.9 40.3 1.0 O2A H:ADP601 4.9 6.9 1.0 N H:ASP61 4.9 41.2 1.0

Fluorine binding site 10 out of 48 in the Cryo-Em Structure of Human Tric-Adp-Alfx


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 10 of Cryo-Em Structure of Human Tric-Adp-Alfx within 5.0Å range: probe atom residue distance (Å) B Occ G:F603 b:6.8 occ:1.00 F1 G:AF3603 0.0 6.8 1.0 AL G:AF3603 1.7 6.8 1.0 O1A G:ADP601 2.7 6.9 1.0 O2A G:ADP601 2.9 6.9 1.0 F2 G:AF3603 2.9 6.8 1.0 F3 G:AF3603 3.0 6.8 1.0 CE G:LYS163 3.0 35.6 1.0 PA G:ADP601 3.2 6.9 1.0 O1B G:ADP601 3.3 6.9 1.0 OG1 G:THR96 3.3 40.4 1.0 O2B G:ADP601 3.4 6.9 1.0 OD1 G:ASP62 3.4 43.5 1.0 MG G:MG602 3.5 9.8 1.0 NZ G:LYS163 3.8 35.6 1.0 PB G:ADP601 3.8 6.9 1.0 OG1 G:THR95 3.8 41.0 1.0 O3A G:ADP601 4.0 6.9 1.0 CD G:LYS163 4.2 35.6 1.0 N G:GLY63 4.3 42.4 1.0 CA G:ASP62 4.4 43.5 1.0 CG G:ASP62 4.4 43.5 1.0 CB G:THR96 4.5 40.4 1.0 O5' G:ADP601 4.6 6.9 1.0 O G:CYS40 4.6 38.7 1.0 CG2 G:THR162 4.7 37.9 1.0 CB G:ASP62 4.8 43.5 1.0 N G:THR96 4.9 40.4 1.0 O G:ASN61 4.9 40.3 1.0 O G:HOH701 4.9 5.0 1.0 C G:ASP62 4.9 43.5 1.0

Y.Cong, C.X.Liu. Pathway and Mechanism of Tubulin Folding Mediated By Tric/Cct Conjugated with Its Atpase Cycle Revealed By Cryo-Em To Be Published.