Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
A | 0016589 | cellular_component | NURF complex |
B | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
B | 0016589 | cellular_component | NURF complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue Y9P A 3101 |
Chain | Residue |
A | PRO2951 |
A | PHE2952 |
A | GLU2954 |
A | TYR3006 |
A | ASN3007 |
A | PHE3013 |
A | HOH3210 |
A | HOH3219 |
B | SER2917 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 3102 |
Chain | Residue |
A | VAL2967 |
A | ILE2968 |
A | LYS2969 |
A | TYR3005 |
A | HOH3237 |
A | HOH3267 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 3103 |
Chain | Residue |
A | ASP2963 |
A | TYR2964 |
A | TYR2965 |
A | GLY2966 |
A | GLN3015 |
A | HOH3206 |
A | HOH3233 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 3104 |
Chain | Residue |
A | HIS2946 |
A | PRO2955 |
A | TYR2965 |
A | GLN3026 |
A | HOH3255 |
A | HOH3288 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue EDO A 3105 |
Chain | Residue |
A | SER2942 |
A | LYS3027 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 3106 |
Chain | Residue |
A | ARG3004 |
A | GLU3018 |
A | GLU3021 |
A | SER3022 |
A | HOH3217 |
A | HOH3261 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO A 3107 |
Chain | Residue |
A | ASP3001 |
A | ARG3004 |
A | TYR3014 |
A | HOH3214 |
A | HOH3261 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue Y9P B 3101 |
Chain | Residue |
A | THR2918 |
B | PRO2951 |
B | PHE2952 |
B | GLU2954 |
B | VAL2956 |
B | ALA2961 |
B | TYR3006 |
B | ASN3007 |
B | PHE3013 |
B | HOH3210 |
B | HOH3218 |
B | HOH3252 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue EDO B 3102 |
Chain | Residue |
B | ASP2963 |
B | TYR2964 |
B | TYR2965 |
B | GLY2966 |
B | GLN3015 |
B | EDO3105 |
B | HOH3246 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue EDO B 3103 |
Chain | Residue |
B | VAL2967 |
B | ILE2968 |
B | LYS2969 |
B | TYR3005 |
B | HOH3230 |
B | HOH3265 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue EDO B 3104 |
Chain | Residue |
B | SER2942 |
B | LYS3027 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue EDO B 3105 |
Chain | Residue |
B | ASP2963 |
B | GLY2966 |
B | GLN3015 |
B | GLU3018 |
B | EDO3102 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue EDO B 3106 |
Chain | Residue |
B | TYR2965 |
B | ARG3004 |
B | GLU3018 |
B | SER3022 |
B | HOH3222 |
B | HOH3290 |
Functional Information from PROSITE/UniProt
site_id | PS00633 |
Number of Residues | 58 |
Details | BROMODOMAIN_1 Bromodomain signature. AwpFlepvDpndap..DYYgvIkepMdlatMeervqrry..Yekltefvadmtk.IfdNCryY |
Chain | Residue | Details |
A | ALA2949-TYR3006 | |