8P1T
Crystal structure of human methionine adenosyltransferase 2A (MAT2A) in complex with SAM and allosteric inhibitor Z237451470
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| AAA | 0004478 | molecular_function | methionine adenosyltransferase activity |
| AAA | 0005515 | molecular_function | protein binding |
| AAA | 0005524 | molecular_function | ATP binding |
| AAA | 0005829 | cellular_component | cytosol |
| AAA | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| AAA | 0006730 | biological_process | one-carbon metabolic process |
| AAA | 0016740 | molecular_function | transferase activity |
| AAA | 0034214 | biological_process | protein hexamerization |
| AAA | 0036094 | molecular_function | small molecule binding |
| AAA | 0042802 | molecular_function | identical protein binding |
| AAA | 0046872 | molecular_function | metal ion binding |
| AAA | 0048269 | cellular_component | methionine adenosyltransferase complex |
| AAA | 0051291 | biological_process | protein heterooligomerization |
| AAA | 0061431 | biological_process | cellular response to methionine |
| AAA | 1904263 | biological_process | positive regulation of TORC1 signaling |
| AAA | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
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 |
| AAA | HIS29 | |
| AAA | ARG264 |
| 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 |
| AAA | ASP31 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0A817 |
| Chain | Residue | Details |
| AAA | GLU57 |
| 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 |
| AAA | GLU70 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: in other chain => ECO:0000305|PubMed:25075345 |
| Chain | Residue | Details |
| AAA | GLN113 |
| 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 |
| AAA | ASP179 |
| 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 |
| AAA | SER247 |
| 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 |
| AAA | ASP258 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0007744|PDB:4NDN |
| Chain | Residue | Details |
| AAA | ALA281 |
| 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 |
| AAA | LYS285 | |
| AAA | ASP291 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | BINDING: in other chain => ECO:0000250|UniProtKB:P0A817 |
| Chain | Residue | Details |
| AAA | LYS289 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| AAA | LYS81 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| AAA | SER114 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| AAA | SER384 |
| 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 |
| AAA | LYS228 | |
| AAA | LYS234 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 14 |
| Details | M-CSA 9 |
| Chain | Residue | Details |
| AAA | HIS29 | proton acceptor, proton donor |
| AAA | ASP31 | electrostatic stabiliser, metal ligand |
| AAA | LYS32 | electrostatic stabiliser |
| AAA | GLU57 | metal ligand |
| AAA | GLU70 | electrostatic stabiliser, steric role |
| AAA | LYS181 | electrostatic stabiliser |
| AAA | PHE250 | steric role |
| AAA | ASP258 | electrostatic stabiliser, metal ligand, steric role |
| AAA | ALA259 | metal ligand |
| AAA | ARG264 | electrostatic stabiliser |
| AAA | LYS265 | electrostatic stabiliser |
| AAA | LYS285 | electrostatic stabiliser |
| AAA | LYS289 | electrostatic stabiliser |
| AAA | ASP291 | electrostatic stabiliser |
