Fluorine in PDB 5gso: Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K

The structure of Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K, PDB code: 5gso was solved by Y.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	95.012, 70.691, 94.931, 90.00, 118.24, 90.00
R / Rfree (%)	21.1 / 28.5

The binding sites of Fluorine atom in the Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K (pdb code 5gso). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 5 binding sites of Fluorine where determined in the Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K, PDB code: 5gso:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5;

Fluorine binding site 1 out of 5 in the Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K within 5.0Å range: probe atom residue distance (Å) B Occ A:F201 b:55.7 occ:1.00 F1 A:5GI201 0.0 55.7 1.0 C9 A:5GI201 1.3 54.7 1.0 C10 A:5GI201 2.3 55.1 1.0 C8 A:5GI201 2.3 53.4 1.0 O A:LYS130 3.3 49.1 1.0 OE1 A:GLU71 3.4 29.4 1.0 OG1 A:THR132 3.5 32.5 1.0 C7 A:5GI201 3.5 54.8 1.0 CB A:LYS130 3.6 44.8 1.0 C6 A:5GI201 3.6 53.0 1.0 NH2 A:ARG39 3.7 30.6 1.0 ND2 A:ASN69 3.8 31.9 1.0 CD A:GLU71 3.8 30.2 1.0 CD A:LYS130 3.9 48.5 1.0 C A:LYS130 4.0 46.5 1.0 C5 A:5GI201 4.0 54.9 1.0 CG A:LYS130 4.2 47.8 1.0 CA A:LYS130 4.4 45.5 1.0 OE2 A:GLU71 4.4 30.2 1.0 O A:PRO131 4.4 41.9 1.0 CG A:GLU71 4.5 28.3 1.0 CB A:THR132 4.8 32.5 1.0 CE A:LYS130 4.8 49.2 1.0 C A:PRO131 4.9 41.6 1.0 CB A:LEU127 4.9 33.0 1.0 CZ A:ARG39 4.9 32.7 1.0 CG A:ASN69 5.0 32.7 1.0

Fluorine binding site 2 out of 5 in the Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K within 5.0Å range: probe atom residue distance (Å) B Occ B:F201 b:56.6 occ:1.00 F1 B:5GI201 0.0 56.6 1.0 C9 B:5GI201 1.3 55.8 1.0 C10 B:5GI201 2.2 57.0 1.0 C8 B:5GI201 2.4 54.4 1.0 OE1 B:GLU71 3.2 25.7 1.0 C7 B:5GI201 3.5 57.3 1.0 NH2 B:ARG39 3.5 37.0 1.0 CB B:LYS130 3.6 47.5 1.0 OG1 B:THR132 3.6 37.6 1.0 C6 B:5GI201 3.6 54.6 1.0 ND2 B:ASN69 3.8 34.2 1.0 CD B:GLU71 3.8 25.1 1.0 O B:LYS130 4.0 47.1 1.0 CD B:LYS130 4.0 43.8 1.0 CG B:LYS130 4.0 44.8 1.0 C5 B:5GI201 4.0 57.3 1.0 OE2 B:GLU71 4.4 23.7 1.0 CG B:GLU71 4.5 24.6 1.0 C B:LYS130 4.5 48.4 1.0 CA B:LYS130 4.6 50.0 1.0 CZ B:ARG39 4.6 37.4 1.0 NE B:ARG39 4.8 35.7 1.0 CB B:GLU71 4.9 26.6 1.0 CG B:ASN69 5.0 35.5 1.0

Fluorine binding site 3 out of 5 in the Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K within 5.0Å range: probe atom residue distance (Å) B Occ C:F201 b:56.8 occ:1.00 F1 C:5GI201 0.0 56.8 1.0 C9 C:5GI201 1.3 56.2 1.0 C10 C:5GI201 2.3 58.0 1.0 C8 C:5GI201 2.3 54.6 1.0 OE1 C:GLU71 3.5 29.5 1.0 CB C:LYS130 3.5 38.0 1.0 C7 C:5GI201 3.5 57.9 1.0 C6 C:5GI201 3.6 54.4 1.0 CD C:LYS130 3.6 41.4 1.0 ND2 C:ASN69 3.8 37.8 1.0 OG1 C:THR132 3.8 34.8 1.0 NH2 C:ARG39 3.8 36.9 1.0 CD C:GLU71 3.9 29.0 1.0 O C:LYS130 3.9 39.0 1.0 C5 C:5GI201 4.1 55.5 1.0 OE2 C:GLU71 4.1 29.2 1.0 CG C:LYS130 4.1 40.6 1.0 C C:LYS130 4.5 37.3 1.0 CA C:LYS130 4.6 38.5 1.0 O C:PRO131 4.7 33.6 1.0 CG C:GLU71 4.8 28.2 1.0 CE C:LYS130 4.9 44.3 1.0 CG C:ASN69 4.9 36.8 1.0 CZ C:ARG39 5.0 37.9 1.0

Fluorine binding site 4 out of 5 in the Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K within 5.0Å range: probe atom residue distance (Å) B Occ D:F201 b:68.0 occ:1.00 F1 D:5GI201 0.0 68.0 1.0 C9 D:5GI201 1.3 66.1 1.0 C10 D:5GI201 2.3 68.1 1.0 C8 D:5GI201 2.3 62.6 1.0 OE1 D:GLU71 3.0 55.7 1.0 ND2 D:ASN69 3.3 59.8 1.0 CD D:GLU71 3.4 54.1 1.0 OG1 D:THR132 3.4 43.6 1.0 C7 D:5GI201 3.6 67.5 1.0 C6 D:5GI201 3.6 61.9 1.0 OE2 D:GLU71 3.8 54.5 1.0 NH2 D:ARG39 3.8 41.6 1.0 O D:LYS130 3.9 60.8 1.0 CD D:LYS130 3.9 60.2 1.0 CG D:LYS130 4.0 61.7 1.0 C5 D:5GI201 4.1 65.9 1.0 CB D:LYS130 4.1 59.0 1.0 CG D:GLU71 4.1 48.5 1.0 O D:PRO131 4.3 50.8 1.0 CE D:LYS130 4.3 60.4 1.0 C D:LYS130 4.5 58.1 1.0 CG D:ASN69 4.5 57.9 1.0 CB D:GLU71 4.7 47.3 1.0 CZ D:ARG39 4.8 48.6 1.0 NE D:ARG39 4.8 50.6 1.0 CB D:THR132 4.9 44.2 1.0 C D:PRO131 4.9 52.2 1.0 CA D:LYS130 5.0 60.1 1.0

Fluorine binding site 5 out of 5 in the Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structures of EV71 3C Protease in Complex with Nk-1.8K within 5.0Å range: probe atom residue distance (Å) B Occ E:F201 b:71.0 occ:1.00 F1 E:5GI201 0.0 71.0 1.0 C9 E:5GI201 1.3 69.9 1.0 C10 E:5GI201 2.3 70.8 1.0 C8 E:5GI201 2.4 68.3 1.0 OE1 E:GLU71 2.9 43.6 1.0 ND2 E:ASN69 3.5 43.3 1.0 OG1 E:THR132 3.5 42.3 1.0 C7 E:5GI201 3.6 70.3 1.0 C6 E:5GI201 3.6 67.8 1.0 CD E:LYS130 3.7 56.1 1.0 NH2 E:ARG39 3.8 44.3 1.0 CD E:GLU71 3.8 44.9 1.0 O E:LYS130 3.9 45.5 1.0 CB E:LYS130 3.9 52.2 1.0 O E:HOH308 4.0 48.5 1.0 CG E:LYS130 4.0 56.2 1.0 C5 E:5GI201 4.1 69.2 1.0 OE2 E:GLU71 4.4 43.6 1.0 C E:LYS130 4.4 47.4 1.0 O E:PRO131 4.5 45.0 1.0 CG E:ASN69 4.6 43.6 1.0 CG E:GLU71 4.8 41.1 1.0 CA E:LYS130 4.8 51.2 1.0 CB E:THR132 4.9 43.0 1.0 C E:PRO131 4.9 44.5 1.0 CZ E:ARG39 5.0 42.2 1.0

Y.Wang, L.Cao, Y.Zhai, Z.Yin, Y.Sun, L.Shang. Structure of the Enterovirus 71 3C Protease in Complex with Nk-1.8K and Indications For the Development of Antienterovirus Protease Inhibitor Antimicrob. Agents V. 61 2017CHEMOTHER..
ISSN: ESSN 1098-6596
PubMed: 28461310
DOI: 10.1128/AAC.00298-17