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 | 2 |
Details | MOD_RES: Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 |
Chain | Residue | Details |
C | THR2003 | |
A | MET1105 | |
A | TYR1142 | |
A | ASN1169 | |
A | CYS1172 | |
A | CYS1225 | |
A | ARG1226 | |
A | CYS1227 | |
A | CYS1232 | |
B | CYS1031 | |
B | CYS1033 | |
D | THR2003 | |
B | CYS1037 | |
B | CYS1042 | |
B | CYS1044 | |
B | CYS1074 | |
B | CYS1078 | |
B | CYS1080 | |
B | CYS1084 | |
B | MET1105 | |
B | TYR1142 | |
B | ASN1169 | |
A | CYS1037 | |
B | CYS1172 | |
B | CYS1225 | |
B | ARG1226 | |
B | CYS1227 | |
B | CYS1232 | |
A | CYS1042 | |
A | CYS1044 | |
A | CYS1074 | |
A | CYS1078 | |
A | CYS1080 | |
A | CYS1084 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
C | LYS2004 | |
D | LYS2004 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594 |
Chain | Residue | Details |
C | GLN2005 | |
D | GLN2005 | |
B | SER973 | |
B | SER1017 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790 |
Chain | Residue | Details |
C | THR2006 | |
D | THR2006 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 |
Chain | Residue | Details |
C | ARG2008 | |
D | ARG2008 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
C | LDH2009 | |
D | LDH2009 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588 |
Chain | Residue | Details |
C | SER2010 | |
D | SER2010 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803 |
Chain | Residue | Details |
C | THR2011 | |
D | THR2011 |