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 | 0016740 | molecular_function | transferase 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 | 0016740 | molecular_function | transferase 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 | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26543159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26543161","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2EX4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5CVD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5CVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5E1D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5E1M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5E1O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5E2A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5E2B","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylthreonine; in N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2004","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 |
