Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004478 | molecular_function | methionine adenosyltransferase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0034214 | biological_process | protein hexamerization |
A | 0036094 | molecular_function | small molecule binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0048269 | cellular_component | methionine adenosyltransferase complex |
A | 0051291 | biological_process | protein heterooligomerization |
A | 0061431 | biological_process | cellular response to methionine |
A | 1904263 | biological_process | positive regulation of TORC1 signaling |
A | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 1 |
Chain | Residue |
A | SAM2 |
A | HIS51 |
A | LYS203 |
A | LYS287 |
A | HOH632 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE SAM A 2 |
Chain | Residue |
A | GLU92 |
A | GLN135 |
A | ASP138 |
A | ILE139 |
A | GLY155 |
A | ASP156 |
A | ASP201 |
A | LYS203 |
A | SER269 |
A | ARG271 |
A | PHE272 |
A | ASP280 |
A | LYS311 |
A | HOH427 |
A | HOH435 |
A | HOH455 |
A | HOH474 |
A | HOH898 |
A | CL1 |
A | HIS51 |
A | PRO52 |
A | ALA77 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: in other chain => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A19 |
Chain | Residue | Details |
A | HIS51 | |
A | ARG286 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4KTT, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A19, ECO:0007744|PDB:5A1G, ECO:0007744|PDB:5A1I |
Chain | Residue | Details |
A | ASP53 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0A817 |
Chain | Residue | Details |
A | GLU79 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: in other chain => ECO:0000305|PubMed:25075345, ECO:0007744|PDB:4NDN |
Chain | Residue | Details |
A | GLU92 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: in other chain => ECO:0000305|PubMed:25075345 |
Chain | Residue | Details |
A | GLN135 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: in other chain => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4KTT, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A19, ECO:0007744|PDB:5A1G, ECO:0007744|PDB:5A1I |
Chain | Residue | Details |
A | ASP201 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | BINDING: in other chain => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4KTT, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A1G, ECO:0007744|PDB:5A1I |
Chain | Residue | Details |
A | SER269 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A1I |
Chain | Residue | Details |
A | ASP280 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0007744|PDB:4NDN |
Chain | Residue | Details |
A | ALA303 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN |
Chain | Residue | Details |
A | LYS307 | |
A | ASP313 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | BINDING: in other chain => ECO:0000250|UniProtKB:P0A817 |
Chain | Residue | Details |
A | LYS311 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS103 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | SER136 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER406 |
site_id | SWS_FT_FI15 |
Number of Residues | 3 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS250 | |
A | LYS256 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1fug |
Chain | Residue | Details |
A | LYS311 | |
A | ASP313 | |
A | LYS307 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1fug |
Chain | Residue | Details |
A | ARG286 | |
A | HIS51 | |
A | LYS287 | |
A | LYS203 |
site_id | MCSA1 |
Number of Residues | 14 |
Details | M-CSA 9 |
Chain | Residue | Details |
A | HIS51 | proton acceptor, proton donor |
A | ARG286 | electrostatic stabiliser |
A | LYS287 | electrostatic stabiliser |
A | LYS307 | electrostatic stabiliser |
A | LYS311 | electrostatic stabiliser |
A | ASP313 | electrostatic stabiliser |
A | ASP53 | electrostatic stabiliser, metal ligand |
A | LYS54 | electrostatic stabiliser |
A | GLU79 | metal ligand |
A | GLU92 | electrostatic stabiliser, steric role |
A | LYS203 | electrostatic stabiliser |
A | PHE272 | steric role |
A | ASP280 | electrostatic stabiliser, metal ligand, steric role |
A | ALA281 | metal ligand |