Zinc in PDB 6gyr: Transcription Factor Dimerization Activates the P300 Acetyltransferase

All present enzymatic activity of Transcription Factor Dimerization Activates the P300 Acetyltransferase:
2.3.1.48;

The structure of Transcription Factor Dimerization Activates the P300 Acetyltransferase, PDB code: 6gyr was solved by D.Panne, E.Ortega, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 3.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	100.826, 146.717, 116.477, 90.00, 91.75, 90.00
R / Rfree (%)	20.9 / 26.5

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 14;

Binding sites:

The binding sites of Zinc atom in the Transcription Factor Dimerization Activates the P300 Acetyltransferase (pdb code 6gyr). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 14 binding sites of Zinc where determined in the Transcription Factor Dimerization Activates the P300 Acetyltransferase, PDB code: 6gyr:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 14 in the Transcription Factor Dimerization Activates the P300 Acetyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Transcription Factor Dimerization Activates the P300 Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1701 b:78.3 occ:1.00 ND1 A:HIS1255 2.2 50.0 1.0 SG A:CYS1164 2.3 49.8 1.0 SG A:CYS1163 2.3 49.5 1.0 SG A:CYS1258 2.5 50.3 1.0 HB2 A:HIS1255 2.7 61.7 1.0 CG A:HIS1255 3.1 51.8 1.0 CE1 A:HIS1255 3.2 48.1 1.0 H A:CYS1164 3.2 56.7 1.0 HB2 A:CYS1258 3.3 49.8 1.0 CB A:HIS1255 3.3 51.4 1.0 HE1 A:HIS1255 3.4 57.7 1.0 H A:HIS1255 3.5 63.8 1.0 CB A:CYS1164 3.5 73.1 1.0 HB2 A:CYS1163 3.5 68.4 1.0 CB A:CYS1258 3.5 41.5 1.0 HB3 A:CYS1164 3.5 87.8 1.0 N A:CYS1164 3.5 47.2 1.0 CB A:CYS1163 3.6 57.0 1.0 HB3 A:CYS1258 3.7 49.8 1.0 HB3 A:HIS1255 3.9 61.7 1.0 CA A:CYS1164 4.0 56.6 1.0 HH2 A:TRP1115 4.2 60.5 1.0 C A:CYS1163 4.2 55.2 1.0 HZ2 A:TRP1115 4.2 67.6 1.0 N A:HIS1255 4.2 53.1 1.0 CD2 A:HIS1255 4.2 64.2 1.0 HB3 A:CYS1163 4.3 68.4 1.0 HD12 A:LEU1168 4.3 90.8 1.0 NE2 A:HIS1255 4.3 62.8 1.0 HB2 A:CYS1164 4.3 87.8 1.0 HH21 A:ARG1645 4.3 56.9 1.0 C A:CYS1164 4.3 50.3 1.0 O A:CYS1164 4.4 57.5 1.0 HD11 A:LEU1168 4.4 90.8 1.0 CA A:HIS1255 4.4 46.5 1.0 CA A:CYS1163 4.5 59.0 1.0 H A:ARG1166 4.5 55.5 1.0 H A:CYS1258 4.8 59.5 1.0 CD1 A:LEU1168 4.8 75.6 1.0 H A:CYS1163 4.8 61.9 1.0 CZ2 A:TRP1115 4.8 56.3 1.0 HB2 A:ARG1166 4.9 83.7 1.0 CH2 A:TRP1115 4.9 50.4 1.0 HA A:CYS1164 4.9 68.0 1.0 NH2 A:ARG1645 4.9 47.3 1.0 CA A:CYS1258 4.9 44.1 1.0 O A:CYS1163 5.0 65.0 1.0

Zinc binding site 2 out of 14 in the Transcription Factor Dimerization Activates the P300 Acetyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Transcription Factor Dimerization Activates the P300 Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1702 b:78.0 occ:1.00 SG A:CYS1272 2.4 64.4 1.0 SG A:CYS1247 2.4 65.4 1.0 SG A:CYS1250 2.4 64.4 1.0 SG A:CYS1275 2.6 67.7 1.0 H A:CYS1250 3.1 69.5 1.0 H A:CYS1272 3.1 63.7 1.0 HB2 A:CYS1247 3.1 74.9 1.0 CB A:CYS1247 3.2 62.3 1.0 HB3 A:CYS1247 3.2 74.9 1.0 HB3 A:CYS1272 3.2 79.9 1.0 HB3 A:CYS1250 3.2 72.8 1.0 HB2 A:CYS1275 3.3 64.6 1.0 CB A:CYS1272 3.4 66.5 1.0 CB A:CYS1250 3.4 60.6 1.0 CB A:CYS1275 3.6 53.8 1.0 H A:CYS1275 3.6 73.2 1.0 N A:CYS1250 3.8 57.8 1.0 N A:CYS1272 3.9 53.0 1.0 HB2 A:GLU1249 4.0 89.6 1.0 HH11 A:ARG1252 4.1 88.9 1.0 HD2 A:ARG1252 4.1 69.2 1.0 HB2 A:CYS1272 4.2 79.9 1.0 CA A:CYS1272 4.2 60.4 1.0 HB2 A:ARG1252 4.2 71.7 1.0 HB2 A:CYS1250 4.2 72.8 1.0 CA A:CYS1250 4.2 59.4 1.0 HB3 A:CYS1275 4.3 64.6 1.0 N A:CYS1275 4.3 61.0 1.0 HE3 A:MET1254 4.4 0.2 1.0 H A:ARG1252 4.5 63.4 1.0 HE1 A:MET1254 4.5 0.2 1.0 H A:GLU1249 4.5 62.8 1.0 CA A:CYS1275 4.6 58.0 1.0 CA A:CYS1247 4.6 55.7 1.0 H A:GLY1251 4.7 69.2 1.0 HA A:VAL1271 4.7 76.8 1.0 HG13 A:VAL1271 4.8 75.4 1.0 O A:CYS1272 4.8 62.2 1.0 C A:CYS1272 4.8 60.8 1.0 NH1 A:ARG1252 4.9 74.1 1.0 CB A:GLU1249 4.9 74.6 1.0 HA A:CYS1247 4.9 66.9 1.0 C A:CYS1250 4.9 53.4 1.0 HA A:CYS1275 4.9 69.6 1.0 CE A:MET1254 4.9 88.4 1.0 C A:GLU1249 5.0 64.9 1.0 HA A:CYS1250 5.0 71.3 1.0

Zinc binding site 3 out of 14 in the Transcription Factor Dimerization Activates the P300 Acetyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Transcription Factor Dimerization Activates the P300 Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1703 b:0.4 occ:1.00 HG A:CYS1177 1.7 0.1 1.0 SG A:CYS1201 2.0 0.7 1.0 SG A:CYS1183 2.2 0.7 1.0 HB3 A:CYS1204 2.8 0.8 1.0 HG A:CYS1201 2.8 0.7 1.0 SG A:CYS1177 2.9 0.6 1.0 HB3 A:CYS1183 3.1 0.4 1.0 HB2 A:LYS1180 3.1 0.6 1.0 CB A:CYS1183 3.1 0.4 1.0 HG A:CYS1204 3.2 0.5 1.0 SG A:CYS1204 3.2 0.6 1.0 HB2 A:CYS1183 3.2 0.4 1.0 HB3 A:CYS1201 3.3 0.6 1.0 CB A:CYS1201 3.4 0.6 1.0 CB A:CYS1204 3.4 0.9 1.0 HB3 A:CYS1177 3.4 0.6 1.0 H A:CYS1201 3.5 0.9 1.0 HB2 A:CYS1177 3.5 0.6 1.0 CB A:CYS1177 3.6 0.7 1.0 HB2 A:CYS1204 3.9 0.8 1.0 H A:CYS1204 3.9 0.7 1.0 H A:LYS1180 3.9 0.0 1.0 HB2 A:CYS1201 4.0 0.6 1.0 CB A:LYS1180 4.0 0.1 1.0 HG2 A:LYS1180 4.1 0.5 1.0 HD3 A:LYS1180 4.2 0.7 1.0 N A:CYS1201 4.2 0.5 1.0 CA A:CYS1201 4.4 0.4 1.0 HB3 A:LYS1180 4.4 0.6 1.0 CG A:LYS1180 4.5 0.8 1.0 CA A:CYS1183 4.6 0.0 1.0 N A:CYS1204 4.6 0.0 1.0 CA A:CYS1204 4.6 0.1 1.0 N A:LYS1180 4.6 0.6 1.0 CD A:LYS1180 4.8 0.5 1.0 H A:THR1184 4.8 0.6 1.0 HA A:CYS1183 4.9 0.7 1.0 HB3 A:LYS1203 5.0 0.1 1.0 CA A:LYS1180 5.0 1.0 1.0

Zinc binding site 4 out of 14 in the Transcription Factor Dimerization Activates the P300 Acetyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Transcription Factor Dimerization Activates the P300 Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1705 b:78.6 occ:1.00 HE2 A:HIS1315 1.6 62.9 1.0 NE2 A:HIS1315 2.2 52.4 1.0 SG A:CYS1408 2.3 66.8 1.0 HD2 A:HIS1315 2.5 45.4 1.0 CD2 A:HIS1315 2.6 37.8 1.0 CB A:CYS1408 3.5 61.9 1.0 CE1 A:HIS1315 3.5 66.9 1.0 HB2 A:CYS1408 3.5 74.3 1.0 HB3 A:CYS1408 3.5 74.3 1.0 CG A:HIS1315 4.0 42.0 1.0 HE1 A:HIS1315 4.0 80.3 1.0 ND1 A:HIS1315 4.3 51.1 1.0 HB2 A:PRO1406 4.5 56.2 1.0 HG A:LEU1409 4.7 48.3 1.0 H A:CYS1408 4.7 49.3 1.0 CA A:CYS1408 4.9 46.5 1.0

Zinc binding site 5 out of 14 in the Transcription Factor Dimerization Activates the P300 Acetyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Transcription Factor Dimerization Activates the P300 Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1701 b:84.0 occ:1.00 ND1 B:HIS1255 2.2 48.0 1.0 SG B:CYS1164 2.2 65.7 1.0 HB2 B:HIS1255 2.4 66.7 1.0 SG B:CYS1163 2.4 61.4 1.0 SG B:CYS1258 2.6 51.2 1.0 CG B:HIS1255 2.9 57.2 1.0 CB B:HIS1255 3.1 55.5 1.0 CE1 B:HIS1255 3.3 59.1 1.0 H B:HIS1255 3.3 66.7 1.0 HB2 B:CYS1258 3.4 71.6 1.0 H B:CYS1164 3.5 87.3 1.0 HE1 B:HIS1255 3.6 71.0 1.0 CB B:CYS1258 3.6 59.6 1.0 HB2 B:CYS1163 3.6 89.0 1.0 HB3 B:HIS1255 3.6 66.7 1.0 CB B:CYS1164 3.7 81.0 1.0 CB B:CYS1163 3.7 74.1 1.0 N B:CYS1164 3.7 72.7 1.0 HB3 B:CYS1258 3.8 71.6 1.0 HB3 B:CYS1164 3.9 97.3 1.0 N B:HIS1255 4.0 55.5 1.0 HH2 B:TRP1115 4.1 74.4 1.0 CD2 B:HIS1255 4.1 64.2 1.0 CA B:HIS1255 4.2 60.3 1.0 CA B:CYS1164 4.2 71.0 1.0 HZ2 B:TRP1115 4.2 89.6 1.0 NE2 B:HIS1255 4.2 65.3 1.0 HD12 B:LEU1168 4.3 73.8 1.0 C B:CYS1163 4.3 55.9 1.0 HB3 B:CYS1163 4.4 89.0 1.0 HB2 B:CYS1164 4.4 97.3 1.0 O B:CYS1164 4.4 61.1 1.0 C B:CYS1164 4.5 58.7 1.0 H B:ARG1166 4.5 76.7 1.0 HH21 B:ARG1645 4.6 59.8 1.0 HD11 B:LEU1168 4.6 73.8 1.0 CA B:CYS1163 4.6 48.0 1.0 H B:CYS1163 4.7 64.2 1.0 HA B:HIS1255 4.7 72.4 1.0 CH2 B:TRP1115 4.8 62.0 1.0 CZ2 B:TRP1115 4.8 74.6 1.0 HB2 B:ARG1166 4.8 68.0 1.0 H B:CYS1258 4.9 65.4 1.0 CD1 B:LEU1168 4.9 61.4 1.0 HD2 B:HIS1255 4.9 77.1 1.0 CA B:CYS1258 5.0 54.9 1.0

Zinc binding site 6 out of 14 in the Transcription Factor Dimerization Activates the P300 Acetyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Transcription Factor Dimerization Activates the P300 Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1702 b:84.0 occ:1.00 SG B:CYS1272 2.4 75.1 1.0 SG B:CYS1275 2.4 68.8 1.0 SG B:CYS1250 2.4 76.7 1.0 SG B:CYS1247 2.5 61.8 1.0 HB3 B:CYS1250 2.6 84.6 1.0 H B:CYS1250 2.8 90.2 1.0 CB B:CYS1250 3.0 70.5 1.0 H B:CYS1272 3.0 72.2 1.0 HB3 B:CYS1247 3.2 67.6 1.0 CB B:CYS1247 3.3 56.2 1.0 HB2 B:CYS1247 3.3 67.6 1.0 HB3 B:CYS1272 3.3 96.7 1.0 CB B:CYS1272 3.4 80.6 1.0 HB2 B:CYS1275 3.4 82.0 1.0 N B:CYS1250 3.5 75.1 1.0 H B:CYS1275 3.6 73.2 1.0 CB B:CYS1275 3.6 68.3 1.0 HB2 B:CYS1250 3.8 84.6 1.0 N B:CYS1272 3.8 60.1 1.0 CA B:CYS1250 3.9 69.8 1.0 HB2 B:GLU1249 3.9 70.9 1.0 CA B:CYS1272 4.1 74.1 1.0 HB2 B:CYS1272 4.2 96.7 1.0 HD2 B:ARG1252 4.3 82.1 1.0 N B:CYS1275 4.3 61.0 1.0 HB3 B:CYS1275 4.3 82.0 1.0 HH11 B:ARG1252 4.3 87.4 1.0 H B:GLY1251 4.4 83.4 1.0 H B:GLU1249 4.5 92.0 1.0 CA B:CYS1275 4.5 64.4 1.0 HA B:CYS1250 4.6 83.9 1.0 HG13 B:VAL1271 4.6 83.1 1.0 HA B:VAL1271 4.6 75.2 1.0 HE1 B:MET1254 4.6 87.4 1.0 O B:CYS1272 4.7 65.6 1.0 H B:ARG1252 4.7 61.7 1.0 C B:CYS1272 4.7 66.3 1.0 HB2 B:ARG1252 4.7 66.0 1.0 CA B:CYS1247 4.7 64.6 1.0 C B:GLU1249 4.7 78.7 1.0 C B:CYS1250 4.8 67.8 1.0 CB B:GLU1249 4.8 59.0 1.0 N B:GLY1251 4.8 69.5 1.0 HE3 B:MET1254 4.8 87.4 1.0 HA B:CYS1275 4.9 77.3 1.0 C B:VAL1271 5.0 53.4 1.0

Zinc binding site 7 out of 14 in the Transcription Factor Dimerization Activates the P300 Acetyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Transcription Factor Dimerization Activates the P300 Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1703 b:0.3 occ:1.00 HB3 B:CYS1183 2.1 0.7 1.0 HG B:CYS1204 2.4 0.1 1.0 CB B:CYS1183 2.4 0.1 1.0 HB2 B:CYS1183 2.4 0.7 1.0 SG B:CYS1183 2.4 0.7 1.0 SG B:CYS1201 2.5 0.4 1.0 HA3 B:GLY1179 2.5 0.5 1.0 HB2 B:CYS1204 2.7 0.0 1.0 HG B:CYS1177 2.8 0.0 1.0 SG B:CYS1204 3.0 0.6 1.0 HB3 B:CYS1201 3.1 0.8 1.0 H B:GLY1179 3.2 0.3 1.0 CB B:CYS1201 3.3 1.0 1.0 CB B:CYS1204 3.3 0.3 1.0 CA B:GLY1179 3.4 0.2 1.0 HB3 B:CYS1177 3.5 0.3 1.0 HB2 B:CYS1201 3.5 0.8 1.0 SG B:CYS1177 3.6 0.5 1.0 HB3 B:CYS1204 3.7 0.0 1.0 N B:GLY1179 3.7 0.8 1.0 H B:LYS1180 3.8 0.2 1.0 CA B:CYS1183 3.9 0.1 1.0 HA2 B:GLY1179 4.0 0.5 1.0 CB B:CYS1177 4.0 0.4 1.0 C B:GLY1179 4.1 0.7 1.0 H B:CYS1204 4.2 0.3 1.0 N B:LYS1180 4.2 0.1 1.0 HA B:CYS1183 4.4 0.6 1.0 HD11 B:ILE1185 4.4 0.3 1.0 H B:CYS1201 4.4 0.3 1.0 H B:CYS1183 4.4 0.9 1.0 HB2 B:CYS1177 4.4 0.3 1.0 HG3 B:LYS1180 4.6 1.0 1.0 C B:CYS1183 4.6 0.1 1.0 CA B:CYS1204 4.6 0.4 1.0 N B:CYS1183 4.7 0.1 1.0 HE1 B:PHE1200 4.7 0.9 1.0 CA B:CYS1201 4.7 0.2 1.0 HD13 B:ILE1185 4.8 0.3 1.0 N B:CYS1204 4.8 0.4 1.0 O B:CYS1183 4.8 0.7 1.0 N B:CYS1201 5.0 0.7 1.0 O B:GLY1179 5.0 0.2 1.0

Zinc binding site 8 out of 14 in the Transcription Factor Dimerization Activates the P300 Acetyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Transcription Factor Dimerization Activates the P300 Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1705 b:92.3 occ:1.00 NE2 B:HIS1315 2.1 56.5 1.0 SG B:CYS1408 2.2 64.3 1.0 NE2 D:HIS1315 2.3 45.5 1.0 SG D:CYS1408 2.5 63.9 1.0 HD2 B:HIS1315 2.8 67.9 1.0 CD2 B:HIS1315 2.8 56.5 1.0 HD2 D:HIS1315 2.9 59.2 1.0 CD2 D:HIS1315 3.0 49.2 1.0 CE1 B:HIS1315 3.3 86.7 1.0 CE1 D:HIS1315 3.4 69.8 1.0 HE1 B:HIS1315 3.6 0.1 1.0 CB B:CYS1408 3.8 57.9 1.0 HE1 D:HIS1315 3.8 83.9 1.0 HB3 B:CYS1408 3.9 69.5 1.0 CB D:CYS1408 3.9 60.2 1.0 HB3 D:CYS1408 4.0 72.3 1.0 HB2 B:CYS1408 4.0 69.5 1.0 CG B:HIS1315 4.1 61.4 1.0 HB2 B:PRO1406 4.2 70.6 1.0 CG D:HIS1315 4.2 45.4 1.0 HB2 D:CYS1408 4.2 72.3 1.0 ND1 B:HIS1315 4.3 71.9 1.0 ND1 D:HIS1315 4.4 62.4 1.0 H B:CYS1408 4.6 44.6 1.0 HG B:LEU1409 4.8 40.7 1.0 HG D:LEU1409 4.8 42.3 1.0 HB2 D:PRO1406 4.9 69.1 1.0 CB B:PRO1406 4.9 58.8 1.0 HG3 B:PRO1406 4.9 63.4 1.0 HB3 B:PRO1406 4.9 70.6 1.0

Zinc binding site 9 out of 14 in the Transcription Factor Dimerization Activates the P300 Acetyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Transcription Factor Dimerization Activates the P300 Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1701 b:88.9 occ:1.00 HD1 C:HIS1255 2.0 92.5 1.0 SG C:CYS1164 2.1 93.1 1.0 SG C:CYS1163 2.1 0.3 1.0 H C:CYS1164 2.2 82.0 1.0 H C:HIS1255 2.6 0.8 1.0 ND1 C:HIS1255 2.7 77.0 1.0 N C:CYS1164 2.9 68.3 1.0 HG C:CYS1258 2.9 92.8 1.0 HB2 C:HIS1255 3.0 0.1 1.0 HB2 C:CYS1258 3.1 95.9 1.0 CB C:CYS1164 3.3 0.0 1.0 HB3 C:CYS1258 3.5 95.9 1.0 N C:HIS1255 3.5 86.5 1.0 CG C:HIS1255 3.5 93.1 1.0 HB3 C:CYS1164 3.5 0.1 1.0 CB C:CYS1258 3.6 79.9 1.0 CA C:CYS1164 3.6 79.5 1.0 CB C:HIS1255 3.6 98.4 1.0 CB C:CYS1163 3.6 0.7 1.0 CE1 C:HIS1255 3.7 87.7 1.0 SG C:CYS1258 3.7 77.3 1.0 H C:CYS1163 3.8 0.6 1.0 HB3 C:MET1254 3.8 0.1 1.0 HB2 C:CYS1163 3.8 0.9 1.0 HA C:MET1254 3.9 0.5 1.0 C C:CYS1163 3.9 90.0 1.0 HE1 C:HIS1255 3.9 0.3 1.0 HZ2 C:TRP1115 4.0 0.5 1.0 O C:CYS1164 4.0 0.0 1.0 C C:CYS1164 4.0 0.0 1.0 CA C:CYS1163 4.1 0.7 1.0 HB2 C:CYS1164 4.1 0.1 1.0 CA C:HIS1255 4.1 95.4 1.0 N C:CYS1163 4.2 0.4 1.0 HB3 C:CYS1163 4.3 0.9 1.0 HB3 C:HIS1255 4.4 0.1 1.0 C C:MET1254 4.5 98.3 1.0 CA C:MET1254 4.5 0.1 1.0 HA C:CYS1164 4.5 95.5 1.0 CB C:MET1254 4.6 88.4 1.0 CD2 C:HIS1255 4.6 85.7 1.0 HH2 C:TRP1115 4.7 0.2 1.0 NE2 C:HIS1255 4.7 80.0 1.0 HG2 C:MET1254 4.7 0.1 1.0 CZ2 C:TRP1115 4.8 92.9 1.0 HA C:HIS1255 4.8 0.6 1.0 HD1 C:TYR1162 4.9 0.1 1.0 N C:GLY1165 4.9 0.5 1.0 O C:HIS1255 4.9 90.5 1.0 O C:CYS1163 5.0 0.8 1.0

Zinc binding site 10 out of 14 in the Transcription Factor Dimerization Activates the P300 Acetyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Transcription Factor Dimerization Activates the P300 Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1702 b:0.1 occ:1.00 SG C:CYS1275 2.4 0.8 1.0 SG C:CYS1250 2.4 0.9 1.0 SG C:CYS1272 2.5 0.5 1.0 SG C:CYS1247 2.7 0.0 1.0 HB2 C:CYS1250 3.0 0.2 1.0 HB2 C:CYS1275 3.2 0.7 1.0 HB3 C:CYS1247 3.3 0.2 1.0 CB C:CYS1250 3.3 0.1 1.0 H C:CYS1272 3.3 0.3 1.0 CB C:CYS1275 3.5 0.7 1.0 CB C:CYS1247 3.5 0.8 1.0 HB2 C:CYS1247 3.7 0.2 1.0 H C:CYS1275 3.7 0.6 1.0 H C:GLU1249 3.9 0.3 1.0 CB C:CYS1272 4.0 0.6 1.0 HB3 C:CYS1250 4.0 0.2 1.0 N C:CYS1250 4.0 0.5 1.0 H C:CYS1250 4.0 0.3 1.0 N C:CYS1272 4.1 0.9 1.0 HB3 C:CYS1275 4.1 0.7 1.0 HB2 C:GLU1249 4.1 0.1 1.0 HB3 C:CYS1272 4.2 0.4 1.0 CA C:CYS1250 4.3 0.9 1.0 C C:GLU1249 4.3 0.3 1.0 N C:CYS1275 4.4 1.0 1.0 CA C:CYS1275 4.5 0.7 1.0 CA C:CYS1272 4.5 0.8 1.0 HG13 C:VAL1271 4.5 0.8 1.0 HH11 C:ARG1252 4.5 0.2 1.0 N C:GLU1249 4.6 0.2 1.0 O C:CYS1272 4.6 0.7 1.0 HB2 C:CYS1272 4.7 0.4 1.0 HA C:CYS1250 4.7 1.0 1.0 HA C:VAL1271 4.7 0.5 1.0 HE3 C:MET1254 4.7 0.9 1.0 O C:GLU1249 4.8 0.8 1.0 CA C:GLU1249 4.8 0.9 1.0 HA C:CYS1275 4.8 0.5 1.0 CB C:GLU1249 4.9 0.2 1.0 C C:CYS1272 4.9 0.7 1.0 HE1 C:MET1254 4.9 0.9 1.0 CA C:CYS1247 4.9 0.8 1.0 HG12 C:VAL1271 4.9 0.8 1.0 H C:THR1248 5.0 0.3 1.0 HB2 C:ARG1252 5.0 0.0 1.0

E.Ortega, S.Rengachari, Z.Ibrahim, N.Hoghoughi, J.Gaucher, A.S.Holehouse, S.Khochbin, D.Panne. Transcription Factor Dimerization Activates the P300 Acetyltransferase. Nature V. 562 538 2018.
ISSN: ESSN 1476-4687
PubMed: 30323286
DOI: 10.1038/S41586-018-0621-1