Zinc in PDB 9uuo: The NUA3 Histone Acetyltransferase Complex

All present enzymatic activity of The NUA3 Histone Acetyltransferase Complex:
2.3.1.48;

The binding sites of Zinc atom in the The NUA3 Histone Acetyltransferase Complex (pdb code 9uuo). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the The NUA3 Histone Acetyltransferase Complex, PDB code: 9uuo:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in the The NUA3 Histone Acetyltransferase Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The NUA3 Histone Acetyltransferase Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn901 b:67.8 occ:1.00 SG A:CYS323 2.3 72.3 1.0 SG A:CYS303 2.4 58.5 1.0 CB A:CYS323 2.7 72.3 1.0 CB A:CYS306 2.8 57.6 1.0 CD2 A:HIS319 2.9 61.6 1.0 NE2 A:HIS319 3.0 61.6 1.0 N A:CYS306 3.4 57.6 1.0 CB A:CYS303 3.5 58.5 1.0 CA A:CYS306 3.7 57.6 1.0 SG A:CYS306 4.2 57.6 1.0 CA A:CYS323 4.2 72.3 1.0 CG A:HIS319 4.3 61.6 1.0 O A:HIS319 4.3 61.6 1.0 CE1 A:HIS319 4.3 61.6 1.0 CB A:PHE305 4.4 57.9 1.0 C A:PHE305 4.5 57.9 1.0 N A:PHE305 4.8 57.9 1.0 C A:CYS306 4.8 57.6 1.0 CA A:PHE305 4.8 57.9 1.0 N A:CYS323 4.8 72.3 1.0 CA A:CYS303 4.9 58.5 1.0 ND1 A:HIS319 4.9 61.6 1.0

Zinc binding site 2 out of 6 in the The NUA3 Histone Acetyltransferase Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The NUA3 Histone Acetyltransferase Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn801 b:119.7 occ:1.00 ND1 B:HIS291 2.2 102.0 1.0 SG B:CYS269 2.4 96.2 1.0 SG B:CYS266 2.5 99.9 1.0 CB B:CYS294 2.5 99.5 1.0 CB B:HIS291 2.5 102.0 1.0 SG B:CYS294 2.6 99.5 1.0 CG B:HIS291 2.7 102.0 1.0 CB B:CYS269 3.3 96.2 1.0 N B:HIS291 3.3 102.0 1.0 CE1 B:HIS291 3.5 102.0 1.0 CA B:HIS291 3.5 102.0 1.0 CB B:CYS266 3.8 99.9 1.0 CA B:CYS294 3.9 99.5 1.0 N B:CYS269 4.0 96.2 1.0 CD2 B:HIS291 4.0 102.0 1.0 CA B:CYS269 4.2 96.2 1.0 NE2 B:HIS291 4.3 102.0 1.0 N B:CYS294 4.4 99.5 1.0 C B:HIS291 4.4 102.0 1.0 O B:HIS291 4.5 102.0 1.0 C B:VAL290 4.6 92.4 1.0 C B:CYS294 4.6 99.5 1.0 CB B:VAL268 4.8 84.5 1.0 O B:CYS294 4.9 99.5 1.0 C B:CYS269 4.9 96.2 1.0

Zinc binding site 3 out of 6 in the The NUA3 Histone Acetyltransferase Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The NUA3 Histone Acetyltransferase Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn802 b:93.6 occ:1.00 ND1 B:HIS340 2.0 77.1 1.0 SG B:CYS343 2.3 84.8 1.0 SG B:CYS320 2.3 89.3 1.0 CB B:CYS323 2.4 99.1 1.0 CG B:HIS340 2.9 77.1 1.0 CE1 B:HIS340 3.0 77.1 1.0 CB B:HIS340 3.1 77.1 1.0 SG B:CYS323 3.5 99.1 1.0 O B:MET322 3.5 93.0 1.0 CB B:CYS343 3.6 84.8 1.0 CB B:CYS320 3.6 89.3 1.0 CA B:CYS323 3.7 99.1 1.0 C B:MET322 3.7 93.0 1.0 CG2 B:THR401 3.7 84.8 1.0 N B:CYS323 3.8 99.1 1.0 CD2 B:HIS340 4.0 77.1 1.0 NE2 B:HIS340 4.1 77.1 1.0 OG1 B:THR401 4.3 84.8 1.0 N B:HIS340 4.3 77.1 1.0 CA B:HIS340 4.3 77.1 1.0 CA B:MET322 4.6 93.0 1.0 CB B:THR401 4.7 84.8 1.0 CB B:MET322 4.7 93.0 1.0 C B:CYS323 4.7 99.1 1.0 N B:MET322 4.8 93.0 1.0 CA B:CYS343 4.8 84.8 1.0 O B:CYS320 4.8 89.3 1.0 CA B:CYS320 4.9 89.3 1.0 N B:THR401 5.0 84.8 1.0 O B:SER325 5.0 100.8 1.0

Zinc binding site 4 out of 6 in the The NUA3 Histone Acetyltransferase Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of The NUA3 Histone Acetyltransferase Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn803 b:146.0 occ:1.00 N B:CYS379 2.1 120.1 1.0 SG B:CYS376 2.3 111.3 1.0 SG B:CYS402 2.4 96.7 1.0 CB B:CYS379 2.5 120.1 1.0 SG B:CYS379 2.5 120.1 1.0 CA B:CYS379 2.8 120.1 1.0 CG2 B:ILE378 2.9 114.1 1.0 CB B:ILE378 3.0 114.1 1.0 C B:ILE378 3.0 114.1 1.0 CB B:CYS402 3.3 96.7 1.0 CA B:ILE378 3.4 114.1 1.0 N B:ILE378 3.8 114.1 1.0 CB B:CYS376 3.9 111.3 1.0 C B:CYS379 3.9 120.1 1.0 ND1 B:HIS399 3.9 93.3 1.0 O B:ILE378 4.0 114.1 1.0 N B:LYS380 4.0 117.5 1.0 CG1 B:ILE378 4.4 114.1 1.0 O B:CYS376 4.6 111.3 1.0 CA B:CYS402 4.6 96.7 1.0 CE1 B:HIS399 4.6 93.3 1.0 C B:CYS376 4.8 111.3 1.0 CG B:PRO324 4.8 102.7 1.0 CG B:HIS399 4.9 93.3 1.0 CA B:CYS376 4.9 111.3 1.0 O B:CYS379 5.0 120.1 1.0

Zinc binding site 5 out of 6 in the The NUA3 Histone Acetyltransferase Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of The NUA3 Histone Acetyltransferase Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn804 b:195.7 occ:1.00 ND1 B:HIS438 2.1 141.8 1.0 SG B:CYS389 2.5 131.8 1.0 CB B:CYS389 2.5 131.8 1.0 SG B:CYS394 2.6 145.4 1.0 CE1 B:HIS438 2.8 141.8 1.0 CB B:CYS435 3.1 134.7 1.0 CG B:HIS438 3.3 141.8 1.0 CG2 B:THR396 3.3 117.8 1.0 CB B:HIS438 3.8 141.8 1.0 CB B:CYS394 3.8 145.4 1.0 N B:CYS435 3.9 134.7 1.0 NE2 B:HIS438 4.0 141.8 1.0 CB B:GLN391 4.0 141.4 1.0 CA B:CYS389 4.0 131.8 1.0 CA B:CYS435 4.1 134.7 1.0 CD2 B:HIS438 4.3 141.8 1.0 SG B:CYS435 4.4 134.7 1.0 CB B:THR396 4.7 117.8 1.0 N B:CYS389 4.7 131.8 1.0 C B:PHE434 4.7 128.7 1.0 C B:CYS389 4.7 131.8 1.0 N B:GLN391 4.7 141.4 1.0 CG B:GLN391 4.9 141.4 1.0

Zinc binding site 6 out of 6 in the The NUA3 Histone Acetyltransferase Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of The NUA3 Histone Acetyltransferase Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn805 b:145.4 occ:1.00 SG B:CYS310 2.4 87.0 1.0 SG B:CYS286 2.5 100.0 1.0 SG B:CYS307 2.5 88.2 1.0 SG B:CYS283 2.7 104.3 1.0 CD1 B:ILE288 2.8 104.1 1.0 CB B:CYS310 3.3 87.0 1.0 CB B:CYS307 3.4 88.2 1.0 CG1 B:ILE288 3.7 104.1 1.0 CB B:CYS283 3.7 104.3 1.0 N B:CYS307 3.9 88.2 1.0 N B:CYS286 4.0 100.0 1.0 CB B:CYS286 4.1 100.0 1.0 N B:CYS310 4.2 87.0 1.0 CA B:CYS307 4.3 88.2 1.0 CA B:CYS310 4.4 87.0 1.0 C B:GLY285 4.5 98.3 1.0 CA B:CYS286 4.6 100.0 1.0 CA B:GLY285 4.6 98.3 1.0 CG2 B:ILE288 4.7 104.1 1.0 O B:CYS286 4.9 100.0 1.0 CB B:ILE288 4.9 104.1 1.0 N B:GLY285 4.9 98.3 1.0

W.P.Shi, Y.R.Wang, H.Q.Zhang. Apo Hat Complex To Be Published.