2EX4
Crystal Structure of Human methyltransferase AD-003 in complex with S-adenosyl-L-homocysteine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006338 | biological_process | chromatin remodeling |
A | 0006480 | biological_process | N-terminal protein amino acid methylation |
A | 0007051 | biological_process | spindle organization |
A | 0007059 | biological_process | chromosome segregation |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008276 | molecular_function | protein methyltransferase activity |
A | 0018013 | biological_process | N-terminal peptidyl-glycine methylation |
A | 0018016 | biological_process | N-terminal peptidyl-proline dimethylation |
A | 0032259 | biological_process | methylation |
A | 0035572 | biological_process | N-terminal peptidyl-serine dimethylation |
A | 0035573 | biological_process | N-terminal peptidyl-serine trimethylation |
A | 0042054 | molecular_function | histone methyltransferase activity |
A | 0071885 | molecular_function | N-terminal protein N-methyltransferase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006338 | biological_process | chromatin remodeling |
B | 0006480 | biological_process | N-terminal protein amino acid methylation |
B | 0007051 | biological_process | spindle organization |
B | 0007059 | biological_process | chromosome segregation |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008276 | molecular_function | protein methyltransferase activity |
B | 0018013 | biological_process | N-terminal peptidyl-glycine methylation |
B | 0018016 | biological_process | N-terminal peptidyl-proline dimethylation |
B | 0032259 | biological_process | methylation |
B | 0035572 | biological_process | N-terminal peptidyl-serine dimethylation |
B | 0035573 | biological_process | N-terminal peptidyl-serine trimethylation |
B | 0042054 | molecular_function | histone methyltransferase activity |
B | 0071885 | molecular_function | N-terminal protein N-methyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE SAH A 1401 |
Chain | Residue |
A | TRP20 |
A | PHE97 |
A | CYS118 |
A | GLY119 |
A | LEU120 |
A | GLN121 |
A | GLN136 |
A | TRP137 |
A | VAL138 |
A | HIS141 |
A | HOH1404 |
A | MET30 |
A | HOH1408 |
A | HOH1410 |
A | GLY70 |
A | GLY72 |
A | ARG75 |
A | ILE76 |
A | ASP92 |
A | ILE93 |
A | THR94 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE SAH B 1402 |
Chain | Residue |
B | TRP20 |
B | MET30 |
B | GLY70 |
B | GLY72 |
B | ARG75 |
B | ILE76 |
B | ASP92 |
B | ILE93 |
B | THR94 |
B | PHE97 |
B | GLY119 |
B | LEU120 |
B | GLN121 |
B | GLN136 |
B | TRP137 |
B | VAL138 |
B | HIS141 |
B | HOH1404 |
B | HOH1409 |
B | HOH1411 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26543159, ECO:0000269|PubMed:26543161, ECO:0007744|PDB:2EX4, ECO:0007744|PDB:5CVD, ECO:0007744|PDB:5CVE, ECO:0007744|PDB:5E1D, ECO:0007744|PDB:5E1M, ECO:0007744|PDB:5E1O, ECO:0007744|PDB:5E2A, ECO:0007744|PDB:5E2B |
Chain | Residue | Details |
A | GLY70 | |
B | GLN136 | |
A | ARG75 | |
A | ASP92 | |
A | LEU120 | |
A | GLN136 | |
B | GLY70 | |
B | ARG75 | |
B | ASP92 | |
B | LEU120 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylthreonine; in N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed => ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895 |
Chain | Residue | Details |
A | THR2 | |
B | THR2 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1or8 |
Chain | Residue | Details |
A | GLN136 | |
A | GLN145 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1or8 |
Chain | Residue | Details |
B | GLN136 | |
B | GLN145 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1or8 |
Chain | Residue | Details |
A | GLY140 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1or8 |
Chain | Residue | Details |
B | GLY140 |