6JM9
cryo-EM structure of DOT1L bound to unmodified nucleosome
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000786 | cellular_component | nucleosome |
| A | 0003677 | molecular_function | DNA binding |
| A | 0030527 | molecular_function | structural constituent of chromatin |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0003677 | molecular_function | DNA binding |
| B | 0030527 | molecular_function | structural constituent of chromatin |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| C | 0000786 | cellular_component | nucleosome |
| C | 0003677 | molecular_function | DNA binding |
| C | 0030527 | molecular_function | structural constituent of chromatin |
| C | 0046982 | molecular_function | protein heterodimerization activity |
| D | 0000786 | cellular_component | nucleosome |
| D | 0003677 | molecular_function | DNA binding |
| D | 0030527 | molecular_function | structural constituent of chromatin |
| D | 0046982 | molecular_function | protein heterodimerization activity |
| E | 0000786 | cellular_component | nucleosome |
| E | 0003677 | molecular_function | DNA binding |
| E | 0030527 | molecular_function | structural constituent of chromatin |
| E | 0046982 | molecular_function | protein heterodimerization activity |
| F | 0003677 | molecular_function | DNA binding |
| F | 0030527 | molecular_function | structural constituent of chromatin |
| F | 0046982 | molecular_function | protein heterodimerization activity |
| G | 0000786 | cellular_component | nucleosome |
| G | 0003677 | molecular_function | DNA binding |
| G | 0030527 | molecular_function | structural constituent of chromatin |
| G | 0046982 | molecular_function | protein heterodimerization activity |
| H | 0000786 | cellular_component | nucleosome |
| H | 0003677 | molecular_function | DNA binding |
| H | 0030527 | molecular_function | structural constituent of chromatin |
| H | 0046982 | molecular_function | protein heterodimerization activity |
| X | 0031151 | molecular_function | histone H3K79 methyltransferase activity |
| X | 0051726 | biological_process | regulation of cell cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for Di-peptide SAM X 500 and GLY X 137 |
| Chain | Residue |
| X | PRO133 |
| X | LYS187 |
| X | ALA188 |
| X | ASP222 |
| X | PHE223 |
| X | LEU224 |
| X | SER225 |
| X | PHE239 |
| X | ASN241 |
| X | PHE245 |
| X | VAL135 |
| X | TYR136 |
| X | GLU138 |
| X | THR139 |
| X | ASP161 |
| X | GLY163 |
| X | SER164 |
| X | GLU186 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide SAM X 500 and PHE X 223 |
| Chain | Residue |
| X | PRO133 |
| X | VAL135 |
| X | TYR136 |
| X | GLY137 |
| X | GLU138 |
| X | THR139 |
| X | ASP161 |
| X | GLY163 |
| X | SER164 |
| X | VAL185 |
| X | GLU186 |
| X | LYS187 |
| X | ALA188 |
| X | ASP222 |
| X | LEU224 |
| X | SER225 |
| X | PHE239 |
| X | ASN241 |
| X | PHE245 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide SAM X 500 and PHE X 223 |
| Chain | Residue |
| X | PRO133 |
| X | VAL135 |
| X | TYR136 |
| X | GLY137 |
| X | GLU138 |
| X | THR139 |
| X | ASP161 |
| X | GLY163 |
| X | SER164 |
| X | VAL185 |
| X | GLU186 |
| X | LYS187 |
| X | ALA188 |
| X | ASP222 |
| X | LEU224 |
| X | SER225 |
| X | PHE239 |
| X | ASN241 |
| X | PHE245 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide SAM X 500 and PHE X 223 |
| Chain | Residue |
| X | PRO133 |
| X | VAL135 |
| X | TYR136 |
| X | GLY137 |
| X | GLU138 |
| X | THR139 |
| X | ASP161 |
| X | GLY163 |
| X | SER164 |
| X | VAL185 |
| X | GLU186 |
| X | LYS187 |
| X | ALA188 |
| X | ASP222 |
| X | LEU224 |
| X | SER225 |
| X | PHE239 |
| X | ASN241 |
| X | PHE245 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide SAM X 500 and LEU X 224 |
| Chain | Residue |
| X | PRO133 |
| X | VAL135 |
| X | TYR136 |
| X | GLY137 |
| X | GLU138 |
| X | THR139 |
| X | ASP161 |
| X | GLY163 |
| X | SER164 |
| X | GLU186 |
| X | LYS187 |
| X | ALA188 |
| X | ASP222 |
| X | PHE223 |
| X | SER225 |
| X | PHE239 |
| X | ASN241 |
| X | PHE245 |
| X | LEU253 |
| X | ARG256 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide SAM X 500 and LEU X 224 |
| Chain | Residue |
| X | GLU138 |
| X | THR139 |
| X | ASP161 |
| X | GLY163 |
| X | SER164 |
| X | GLU186 |
| X | LYS187 |
| X | ALA188 |
| X | ASP222 |
| X | PHE223 |
| X | SER225 |
| X | PHE239 |
| X | ASN241 |
| X | PHE245 |
| X | LEU253 |
| X | ARG256 |
| X | PRO133 |
| X | VAL135 |
| X | TYR136 |
| X | GLY137 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide SAM X 500 and LEU X 224 |
| Chain | Residue |
| X | PRO133 |
| X | VAL135 |
| X | TYR136 |
| X | GLY137 |
| X | GLU138 |
| X | THR139 |
| X | ASP161 |
| X | GLY163 |
| X | SER164 |
| X | GLU186 |
| X | LYS187 |
| X | ALA188 |
| X | ASP222 |
| X | PHE223 |
| X | SER225 |
| X | PHE239 |
| X | ASN241 |
| X | PHE245 |
| X | LEU253 |
| X | ARG256 |
Functional Information from PROSITE/UniProt
| site_id | PS00357 |
| Number of Residues | 23 |
| Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
| Chain | Residue | Details |
| D | ARG89-GLY111 |
| site_id | PS00046 |
| Number of Residues | 7 |
| Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
| Chain | Residue | Details |
| C | ALA21-VAL27 |
| site_id | PS00959 |
| Number of Residues | 9 |
| Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
| Chain | Residue | Details |
| A | PRO66-ILE74 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| X | TYR136 | |
| X | PHE159 | |
| X | GLU186 | |
| X | ASP222 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| X | SER297 | |
| B | LYS44 | |
| H | LYS117 | |
| F | LYS16 | |
| F | LYS44 | |
| F | LYS79 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 |
| Chain | Residue | Details |
| B | LYS20 | |
| F | LYS20 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 |
| Chain | Residue | Details |
| B | LYS31 | |
| B | LYS91 | |
| F | LYS31 | |
| F | LYS91 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 |
| Chain | Residue | Details |
| B | SER47 | |
| F | SER47 | |
| E | THR80 | |
| E | THR107 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62805 |
| Chain | Residue | Details |
| B | TYR51 | |
| B | TYR88 | |
| F | TYR51 | |
| F | TYR88 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 |
| Chain | Residue | Details |
| B | LYS59 | |
| F | LYS59 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805 |
| Chain | Residue | Details |
| B | LYS77 | |
| F | LYS77 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805 |
| Chain | Residue | Details |
| B | LYS31 | |
| F | LYS31 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 |
| Chain | Residue | Details |
| B | LYS91 | |
| F | LYS91 |
