Zinc in PDB 4zft: Catalytic Domain of SST2 F403W Mutant Bound to Ubiquitin

The structure of Catalytic Domain of SST2 F403W Mutant Bound to Ubiquitin, PDB code: 4zft was solved by A.N.Bueno, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.19 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.820, 89.397, 117.822, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 23.5

The binding sites of Zinc atom in the Catalytic Domain of SST2 F403W Mutant Bound to Ubiquitin (pdb code 4zft). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Catalytic Domain of SST2 F403W Mutant Bound to Ubiquitin, PDB code: 4zft:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Catalytic Domain of SST2 F403W Mutant Bound to Ubiquitin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Catalytic Domain of SST2 F403W Mutant Bound to Ubiquitin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:35.1 occ:1.00 OXT B:GLY76 1.9 44.2 1.0 OD2 A:ASP354 2.1 37.5 1.0 NE2 A:HIS341 2.2 33.2 1.0 NE2 A:HIS343 2.2 36.3 1.0 C B:GLY76 2.6 41.4 1.0 CG A:ASP354 2.8 33.8 1.0 OD1 A:ASP354 2.8 29.5 1.0 O B:GLY76 2.9 45.8 1.0 CE1 A:HIS341 3.0 25.9 1.0 CD2 A:HIS343 3.1 28.8 1.0 CD2 A:HIS341 3.3 29.2 1.0 CE1 A:HIS343 3.3 34.3 1.0 CA B:GLY76 3.9 38.8 1.0 N B:GLY76 3.9 37.9 1.0 OG A:SER351 4.1 33.5 1.0 ND1 A:HIS341 4.2 32.7 1.0 CB A:ASP354 4.2 28.3 1.0 CG A:HIS343 4.3 38.1 1.0 CG A:HIS341 4.3 27.2 1.0 ND1 A:HIS343 4.4 38.8 1.0 O A:PHE349 4.4 33.8 1.0 N A:SER351 4.5 30.1 1.0 CB A:SER351 4.5 34.2 1.0 O B:HOH205 4.7 45.2 1.0 CG1 A:VAL372 4.8 34.1 1.0 C B:GLY75 5.0 38.2 1.0 CG2 A:VAL372 5.0 33.5 1.0 OE1 A:GLU286 5.0 41.6 1.0

Zinc binding site 2 out of 4 in the Catalytic Domain of SST2 F403W Mutant Bound to Ubiquitin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Catalytic Domain of SST2 F403W Mutant Bound to Ubiquitin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:36.4 occ:1.00 NE2 A:HIS356 2.1 37.2 1.0 NE2 A:HIS404 2.1 39.4 1.0 NE2 A:HIS406 2.1 38.9 1.0 SG A:CYS397 2.3 40.7 1.0 CE1 A:HIS406 2.9 41.1 1.0 CD2 A:HIS356 3.0 26.7 1.0 CD2 A:HIS404 3.0 44.2 1.0 CE1 A:HIS356 3.1 33.9 1.0 CE1 A:HIS404 3.2 43.7 1.0 CD2 A:HIS406 3.2 36.3 1.0 CB A:CYS397 3.4 35.9 1.0 ND1 A:HIS406 4.1 40.2 1.0 CG A:HIS356 4.2 35.0 1.0 CG A:HIS404 4.2 48.2 1.0 ND1 A:HIS356 4.2 33.2 1.0 ND1 A:HIS404 4.2 41.8 1.0 CG A:HIS406 4.2 42.4 1.0 CD1 A:ILE394 4.4 37.3 1.0 OG A:SER352 4.5 48.6 1.0 CA A:CYS397 4.8 36.6 1.0 CB A:LYS399 4.8 39.2 1.0 C A:CYS397 4.9 44.2 1.0

Zinc binding site 3 out of 4 in the Catalytic Domain of SST2 F403W Mutant Bound to Ubiquitin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Catalytic Domain of SST2 F403W Mutant Bound to Ubiquitin within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn501 b:49.0 occ:1.00 O D:GLY76 1.8 40.1 1.0 OD2 C:ASP354 1.9 47.1 1.0 NE2 C:HIS343 2.0 51.1 1.0 NE2 C:HIS341 2.2 51.3 1.0 CG C:ASP354 2.7 43.3 1.0 CE1 C:HIS343 2.8 55.2 1.0 OD1 C:ASP354 2.9 44.8 1.0 C D:GLY76 3.0 50.8 1.0 CE1 C:HIS341 3.0 45.4 1.0 CD2 C:HIS343 3.2 56.0 1.0 CD2 C:HIS341 3.3 42.1 1.0 N D:GLY76 3.8 45.9 1.0 CA D:GLY76 3.9 52.3 1.0 ND1 C:HIS343 4.0 56.8 1.0 OG C:SER351 4.0 47.6 1.0 CB C:ASP354 4.1 38.3 1.0 CG C:HIS343 4.2 56.5 1.0 ND1 C:HIS341 4.2 46.4 1.0 CB C:SER351 4.3 49.2 1.0 N C:SER351 4.3 45.3 1.0 O C:PHE349 4.4 49.7 1.0 CG C:HIS341 4.4 46.1 1.0 CG1 C:VAL372 4.8 47.0 1.0 C D:GLY75 5.0 49.3 1.0 CA C:SER351 5.0 46.6 1.0

Zinc binding site 4 out of 4 in the Catalytic Domain of SST2 F403W Mutant Bound to Ubiquitin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Catalytic Domain of SST2 F403W Mutant Bound to Ubiquitin within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn502 b:47.6 occ:1.00 NE2 C:HIS406 2.0 46.4 1.0 NE2 C:HIS356 2.0 46.6 1.0 NE2 C:HIS404 2.1 52.1 1.0 SG C:CYS397 2.3 49.2 1.0 CE1 C:HIS356 2.9 48.4 1.0 CE1 C:HIS406 2.9 53.5 1.0 CD2 C:HIS406 3.0 48.2 1.0 CD2 C:HIS404 3.0 54.4 1.0 CD2 C:HIS356 3.1 39.0 1.0 CE1 C:HIS404 3.1 55.6 1.0 CB C:CYS397 3.4 47.6 1.0 ND1 C:HIS406 4.0 55.0 1.0 ND1 C:HIS356 4.1 38.1 1.0 CG C:HIS406 4.1 56.8 1.0 CG C:HIS404 4.2 58.4 1.0 CG C:HIS356 4.2 44.6 1.0 ND1 C:HIS404 4.2 57.9 1.0 OG C:SER352 4.3 53.6 1.0 CD1 C:ILE394 4.4 40.4 1.0 CA C:CYS397 4.7 49.0 1.0 C C:CYS397 4.8 57.6 1.0 O C:CYS397 4.9 49.5 1.0 CB C:LYS399 4.9 57.6 1.0

A.N.Bueno, A.N.Bueno. N/A N/A.