7KDB
Crystal structure of human methionine adenosyltransferase 2A (MAT2A) in complex with SAM and allosteric inhibitor compound 35
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 | 17 |
| Details | binding site for residue WBS A 401 |
| Chain | Residue |
| A | PHE18 |
| A | LEU315 |
| A | SER331 |
| A | ILE332 |
| A | PHE333 |
| A | GLU342 |
| A | EDO408 |
| A | HOH560 |
| A | HOH801 |
| A | PHE20 |
| A | GLN190 |
| A | ARG192 |
| A | GLY193 |
| A | ALA194 |
| A | GLY273 |
| A | TRP274 |
| A | ARG313 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | HIS29 |
| A | ASP134 |
| A | LYS181 |
| A | LYS265 |
| A | SAM409 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue TRS A 403 |
| Chain | Residue |
| A | ALA86 |
| A | GLN372 |
| A | HOH608 |
| A | HOH640 |
| A | HOH855 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | GLY91 |
| A | LYS97 |
| A | ARG168 |
| A | LEU176 |
| A | ARG177 |
| A | PRO178 |
| A | HOH521 |
| A | HOH842 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | ARG219 |
| A | HIS243 |
| A | LEU244 |
| A | PRO246 |
| A | HOH513 |
| A | HOH654 |
| A | HOH848 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | ASP124 |
| A | ARG125 |
| A | ASN126 |
| A | LYS228 |
| A | ALA229 |
| A | VAL230 |
| A | VAL231 |
| A | PRO232 |
| A | HOH504 |
| A | HOH566 |
| A | HOH619 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 407 |
| Chain | Residue |
| A | ARG177 |
| A | GLU211 |
| A | HOH507 |
| A | HOH693 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | GLY193 |
| A | PHE333 |
| A | TYR335 |
| A | WBS401 |
| A | HOH524 |
| A | HOH583 |
| A | HOH636 |
| A | HOH636 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | binding site for residue SAM A 409 |
| Chain | Residue |
| A | HIS29 |
| A | PRO30 |
| A | ALA55 |
| A | GLU70 |
| A | GLN113 |
| A | ASP116 |
| A | ILE117 |
| A | GLY133 |
| A | ASP134 |
| A | ASP179 |
| A | LYS181 |
| A | SER247 |
| A | ARG249 |
| A | PHE250 |
| A | ASP258 |
| A | LYS289 |
| A | CL402 |
| A | HOH609 |
| A | HOH663 |
| A | HOH667 |
| A | HOH680 |
| A | HOH736 |
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 |
