7BHU
Crystal structure of MAT2a with elaborated fragment 26 bound in the allosteric site
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
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 | 0031503 | biological_process | protein-containing complex localization |
A | 0031669 | biological_process | cellular response to nutrient levels |
A | 0034198 | biological_process | cellular response to amino acid starvation |
A | 0034214 | biological_process | protein hexamerization |
A | 0036094 | molecular_function | small molecule binding |
A | 0038202 | biological_process | TORC1 signaling |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0048269 | cellular_component | methionine adenosyltransferase complex |
A | 0051259 | biological_process | protein complex oligomerization |
A | 0051291 | biological_process | protein heterooligomerization |
A | 0061431 | biological_process | cellular response to methionine |
A | 0061462 | biological_process | protein localization to lysosome |
A | 1904262 | biological_process | negative regulation of TORC1 signaling |
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 | 14 |
Details | binding site for residue TOW A 401 |
Chain | Residue |
A | PHE18 |
A | PHE333 |
A | TYR335 |
A | EDO403 |
A | EDO403 |
A | HOH579 |
A | PHE20 |
A | PHE139 |
A | GLN190 |
A | GLY273 |
A | TRP274 |
A | GLY275 |
A | ARG313 |
A | GLN317 |
site_id | AC2 |
Number of Residues | 21 |
Details | binding site for residue SAM A 402 |
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 | HOH552 |
A | HOH592 |
A | HOH639 |
A | HOH640 |
A | HOH703 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | GLY275 |
A | GLY275 |
A | TYR335 |
A | TYR335 |
A | TOW401 |
A | TOW401 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | Region: {"description":"Flexible loop","evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A19","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4KTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A19","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1I","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4KTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A19","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1I","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4KTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1I","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1I","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 3 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
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 |