7KDA
Crystal structure of human methionine adenosyltransferase 2A (MAT2A) in complex with SAM and allosteric inhibitor compound 34
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 | 22 |
Details | binding site for residue SAM A 501 |
Chain | Residue |
A | HIS29 |
A | ASP179 |
A | LYS181 |
A | SER247 |
A | ARG249 |
A | PHE250 |
A | ASP258 |
A | LYS289 |
A | CL502 |
A | HOH715 |
A | HOH747 |
A | PRO30 |
A | HOH757 |
A | HOH784 |
A | HOH813 |
A | ALA55 |
A | GLU70 |
A | GLN113 |
A | ASP116 |
A | ILE117 |
A | GLY133 |
A | ASP134 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CL A 502 |
Chain | Residue |
A | HIS29 |
A | ASP134 |
A | LYS181 |
A | LYS265 |
A | SAM501 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue TRS A 503 |
Chain | Residue |
A | GLU85 |
A | ALA86 |
A | HIS89 |
A | GLN372 |
A | HOH645 |
A | HOH704 |
A | HOH708 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | ASP124 |
A | ARG125 |
A | ASN126 |
A | ALA229 |
A | VAL230 |
A | VAL231 |
A | PRO232 |
A | HOH632 |
A | HOH660 |
A | HOH686 |
A | HOH739 |
A | HOH877 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue WBM A 505 |
Chain | Residue |
A | PHE18 |
A | PHE20 |
A | GLN190 |
A | GLY273 |
A | TRP274 |
A | ARG313 |
A | LEU315 |
A | SER331 |
A | ILE332 |
A | PHE333 |
A | GLU342 |
A | HOH627 |
A | HOH822 |
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 | HIS29 | |
A | 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 |
A | ASP31 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0A817 |
Chain | Residue | Details |
A | 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 |
A | GLU70 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: in other chain => ECO:0000305|PubMed:25075345 |
Chain | Residue | Details |
A | 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 |
A | 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 |
A | 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 |
A | ASP258 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0007744|PDB:4NDN |
Chain | Residue | Details |
A | 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 |
A | LYS285 | |
A | ASP291 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | BINDING: in other chain => ECO:0000250|UniProtKB:P0A817 |
Chain | Residue | Details |
A | LYS289 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS81 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | SER114 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | 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 |
A | LYS228 | |
A | LYS234 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 14 |
Details | M-CSA 9 |
Chain | Residue | Details |
A | HIS29 | proton acceptor, proton donor |
A | ARG264 | electrostatic stabiliser |
A | LYS265 | electrostatic stabiliser |
A | LYS285 | electrostatic stabiliser |
A | LYS289 | electrostatic stabiliser |
A | ASP291 | electrostatic stabiliser |
A | ASP31 | electrostatic stabiliser, metal ligand |
A | LYS32 | electrostatic stabiliser |
A | GLU57 | metal ligand |
A | GLU70 | electrostatic stabiliser, steric role |
A | LYS181 | electrostatic stabiliser |
A | PHE250 | steric role |
A | ASP258 | electrostatic stabiliser, metal ligand, steric role |
A | ALA259 | metal ligand |