4I51
Methyltransferase domain of HUMAN EUCHROMATIC HISTONE METHYLTRANSFERASE 1, mutant Y1211A
Replaces: 4H4HFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002039 | molecular_function | p53 binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| A | 0042054 | molecular_function | histone methyltransferase activity |
| A | 0046974 | molecular_function | histone H3K9 methyltransferase activity |
| B | 0002039 | molecular_function | p53 binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| B | 0042054 | molecular_function | histone methyltransferase activity |
| B | 0046974 | molecular_function | histone H3K9 methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SAH A 3001 |
| Chain | Residue |
| A | MET1105 |
| A | HIS1170 |
| A | PHE1215 |
| A | LYS1219 |
| A | PHE1223 |
| A | CYS1225 |
| A | ARG1226 |
| A | HOH3151 |
| A | HOH3173 |
| A | HOH3215 |
| A | HOH3314 |
| A | GLY1106 |
| C | LDH2009 |
| A | TRP1107 |
| A | SER1141 |
| A | TYR1142 |
| A | ARG1166 |
| A | PHE1167 |
| A | ILE1168 |
| A | ASN1169 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 3002 |
| Chain | Residue |
| A | CYS1031 |
| A | CYS1044 |
| A | CYS1074 |
| A | CYS1078 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 3003 |
| Chain | Residue |
| A | CYS1037 |
| A | CYS1074 |
| A | CYS1080 |
| A | CYS1084 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 3004 |
| Chain | Residue |
| A | CYS1031 |
| A | CYS1033 |
| A | CYS1037 |
| A | CYS1042 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 3005 |
| Chain | Residue |
| A | CYS1172 |
| A | CYS1225 |
| A | CYS1227 |
| A | CYS1232 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 3006 |
| Chain | Residue |
| A | ASN1013 |
| A | ILE1021 |
| A | ARG1023 |
| B | HOH3266 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 3007 |
| Chain | Residue |
| A | CYS1033 |
| A | ILE1034 |
| A | ASP1035 |
| A | SER1039 |
| A | ASN1041 |
| A | HOH3365 |
| B | LEU1047 |
| B | LEU1070 |
| B | PHE1072 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SAH B 3001 |
| Chain | Residue |
| B | MET1105 |
| B | GLY1106 |
| B | TRP1107 |
| B | SER1141 |
| B | TYR1142 |
| B | ARG1166 |
| B | PHE1167 |
| B | ASN1169 |
| B | HIS1170 |
| B | PHE1223 |
| B | CYS1225 |
| B | ARG1226 |
| B | HOH3206 |
| D | LDH2009 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 3002 |
| Chain | Residue |
| B | CYS1031 |
| B | CYS1044 |
| B | CYS1074 |
| B | CYS1078 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 3003 |
| Chain | Residue |
| B | CYS1037 |
| B | CYS1074 |
| B | CYS1080 |
| B | CYS1084 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 3004 |
| Chain | Residue |
| B | CYS1031 |
| B | CYS1033 |
| B | CYS1037 |
| B | CYS1042 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 3005 |
| Chain | Residue |
| B | CYS1172 |
| B | CYS1225 |
| B | CYS1227 |
| B | CYS1232 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 3006 |
| Chain | Residue |
| A | ARG1023 |
| A | HOH3123 |
| B | ARG1023 |
| B | LEU1128 |
| B | HOH3155 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 126 |
| Details | Domain: {"description":"Pre-SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00157","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 117 |
| Details | Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 25 |
| Details | Region: {"description":"Interaction with histone H3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 36 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Histone H3K9me binding","evidences":[{"source":"PubMed","id":"18264113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20084102","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by HASPIN and VRK1","evidences":[{"source":"PubMed","id":"15681610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16185088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31527692","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16267050","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16457588","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"5-glutamyl serotonin; alternate","evidences":[{"source":"PubMed","id":"30867594","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by PKC","evidences":[{"source":"PubMed","id":"20228790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Symmetric dimethylarginine; by PRMT5; alternate","evidences":[{"source":"UniProtKB","id":"P68433","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






