5VSD
Structure of human GLP SET-domain (EHMT1) in complex with inhibitor 13
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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue SAM A 3001 |
| Chain | Residue |
| A | MET1136 |
| A | TYR1242 |
| A | PHE1246 |
| A | CYS1256 |
| A | ARG1257 |
| A | HOH3125 |
| A | HOH3177 |
| A | HOH3202 |
| A | HOH3226 |
| A | HOH3261 |
| A | HOH3287 |
| A | GLY1137 |
| A | TRP1138 |
| A | SER1172 |
| A | TYR1173 |
| A | ARG1197 |
| A | PHE1198 |
| A | ASN1200 |
| A | HIS1201 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 3002 |
| Chain | Residue |
| A | CYS1062 |
| A | CYS1075 |
| A | CYS1105 |
| A | CYS1109 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 3003 |
| Chain | Residue |
| A | CYS1068 |
| A | CYS1105 |
| A | CYS1111 |
| A | CYS1115 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 3004 |
| Chain | Residue |
| A | CYS1062 |
| A | CYS1064 |
| A | CYS1068 |
| A | CYS1073 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 3005 |
| Chain | Residue |
| A | CYS1203 |
| A | CYS1256 |
| A | CYS1258 |
| A | CYS1263 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue 9HJ A 3006 |
| Chain | Residue |
| A | ASP1162 |
| A | ALA1165 |
| A | ASP1166 |
| A | ARG1168 |
| A | ASP1171 |
| A | LEU1174 |
| A | ASP1176 |
| A | CYS1186 |
| A | ARG1245 |
| A | PHE1246 |
| A | ILE1249 |
| A | LYS1250 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue DIO A 3007 |
| Chain | Residue |
| A | CYS1064 |
| A | ILE1065 |
| A | ASP1066 |
| A | ASN1072 |
| B | LEU1078 |
| B | PHE1103 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | binding site for residue SAM B 3001 |
| Chain | Residue |
| B | MET1136 |
| B | GLY1137 |
| B | TRP1138 |
| B | SER1172 |
| B | TYR1173 |
| B | ARG1197 |
| B | PHE1198 |
| B | ASN1200 |
| B | HIS1201 |
| B | TYR1242 |
| B | CYS1256 |
| B | ARG1257 |
| B | HOH3216 |
| B | HOH3222 |
| B | HOH3249 |
| B | HOH3263 |
| B | HOH3285 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 3002 |
| Chain | Residue |
| B | CYS1062 |
| B | CYS1075 |
| B | CYS1105 |
| B | CYS1109 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 3003 |
| Chain | Residue |
| B | CYS1068 |
| B | CYS1105 |
| B | CYS1111 |
| B | CYS1115 |
| B | ZN3004 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 3004 |
| Chain | Residue |
| B | CYS1062 |
| B | CYS1064 |
| B | CYS1068 |
| B | CYS1073 |
| B | ZN3003 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 3005 |
| Chain | Residue |
| B | CYS1203 |
| B | CYS1256 |
| B | CYS1258 |
| B | CYS1263 |
| site_id | AD4 |
| Number of Residues | 10 |
| Details | binding site for residue 9HJ B 3006 |
| Chain | Residue |
| B | ALA1165 |
| B | ASP1166 |
| B | ARG1168 |
| B | ASP1171 |
| B | LEU1174 |
| B | ASP1176 |
| B | ARG1245 |
| B | PHE1246 |
| B | ILE1249 |
| B | LYS1250 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 3007 |
| Chain | Residue |
| A | HOH3260 |
| B | ARG1054 |
| A | HOH3159 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 3008 |
| Chain | Residue |
| B | ASN1044 |
| B | LEU1159 |
| B | LEU1177 |
| B | HIS1216 |
| B | PHE1221 |
| B | PRO1222 |
| B | ARG1223 |
| B | HOH3254 |
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 | 6 |
| Details | Region: {"description":"Interaction with histone H3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| 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_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
