8XPT
The Crystal Structure of EHMT1 from Biortus.
Functional 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 |
| C | 0002039 | molecular_function | p53 binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| C | 0042054 | molecular_function | histone methyltransferase activity |
| C | 0046974 | molecular_function | histone H3K9 methyltransferase activity |
| D | 0002039 | molecular_function | p53 binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| D | 0042054 | molecular_function | histone methyltransferase activity |
| D | 0046974 | molecular_function | histone H3K9 methyltransferase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 68 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS1062 | |
| A | MET1136 | |
| A | TYR1173 | |
| A | ASN1200 | |
| A | CYS1203 | |
| A | CYS1256 | |
| A | ARG1257 | |
| A | CYS1258 | |
| A | CYS1263 | |
| B | CYS1062 | |
| B | CYS1064 | |
| A | CYS1064 | |
| B | CYS1068 | |
| B | CYS1073 | |
| B | CYS1075 | |
| B | CYS1105 | |
| B | CYS1109 | |
| B | CYS1111 | |
| B | CYS1115 | |
| B | MET1136 | |
| B | TYR1173 | |
| B | ASN1200 | |
| A | CYS1068 | |
| B | CYS1203 | |
| B | CYS1256 | |
| B | ARG1257 | |
| B | CYS1258 | |
| B | CYS1263 | |
| C | CYS1062 | |
| C | CYS1064 | |
| C | CYS1068 | |
| C | CYS1073 | |
| C | CYS1075 | |
| A | CYS1073 | |
| C | CYS1105 | |
| C | CYS1109 | |
| C | CYS1111 | |
| C | CYS1115 | |
| C | MET1136 | |
| C | TYR1173 | |
| C | ASN1200 | |
| C | CYS1203 | |
| C | CYS1256 | |
| C | ARG1257 | |
| A | CYS1075 | |
| C | CYS1258 | |
| C | CYS1263 | |
| D | CYS1062 | |
| D | CYS1064 | |
| D | CYS1068 | |
| D | CYS1073 | |
| D | CYS1075 | |
| D | CYS1105 | |
| D | CYS1109 | |
| D | CYS1111 | |
| A | CYS1105 | |
| D | CYS1115 | |
| D | MET1136 | |
| D | TYR1173 | |
| D | ASN1200 | |
| D | CYS1203 | |
| D | CYS1256 | |
| D | ARG1257 | |
| D | CYS1258 | |
| D | CYS1263 | |
| A | CYS1109 | |
| A | CYS1111 | |
| A | CYS1115 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Histone H3K9me binding => ECO:0000269|PubMed:18264113, ECO:0000269|PubMed:20084102 |
| Chain | Residue | Details |
| A | TYR1155 | |
| B | TYR1155 | |
| C | TYR1155 | |
| D | TYR1155 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER1004 | |
| A | SER1048 | |
| B | SER1004 | |
| B | SER1048 | |
| C | SER1004 | |
| C | SER1048 | |
| D | SER1004 | |
| D | SER1048 |
