4PAA
Crystal structure of the mature form of rat DMGDH complexed with tetrahydrofolate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005542 | molecular_function | folic acid binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0006579 | biological_process | amino-acid betaine catabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019695 | biological_process | choline metabolic process |
A | 0035999 | biological_process | tetrahydrofolate interconversion |
A | 0042426 | biological_process | choline catabolic process |
A | 0047865 | molecular_function | dimethylglycine dehydrogenase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0005542 | molecular_function | folic acid binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0006579 | biological_process | amino-acid betaine catabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019695 | biological_process | choline metabolic process |
B | 0035999 | biological_process | tetrahydrofolate interconversion |
B | 0042426 | biological_process | choline catabolic process |
B | 0047865 | molecular_function | dimethylglycine dehydrogenase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 36 |
Details | binding site for residue FAD A 901 |
Chain | Residue |
A | ILE48 |
A | GLY80 |
A | SER81 |
A | THR82 |
A | HIS84 |
A | ALA85 |
A | ALA86 |
A | GLY87 |
A | LEU88 |
A | VAL212 |
A | ALA241 |
A | GLY49 |
A | GLY242 |
A | TRP244 |
A | HIS263 |
A | TYR265 |
A | GLY363 |
A | PRO364 |
A | ILE365 |
A | PHE390 |
A | TYR392 |
A | GLY393 |
A | GLY51 |
A | ILE394 |
A | ILE395 |
A | HOH1018 |
A | HOH1021 |
A | HOH1048 |
A | HOH1072 |
A | HOH1102 |
A | CYS52 |
A | VAL53 |
A | LEU72 |
A | GLU73 |
A | LYS74 |
A | ALA79 |
site_id | AC2 |
Number of Residues | 14 |
Details | binding site for residue THG A 902 |
Chain | Residue |
A | PHE530 |
A | ILE560 |
A | GLU573 |
A | THR575 |
A | ILE587 |
A | PHE649 |
A | LEU650 |
A | TYR669 |
A | GLU676 |
A | TYR678 |
A | PHE717 |
A | TYR737 |
A | THR843 |
A | HOH1057 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue THG B 902 |
Chain | Residue |
B | PHE530 |
B | ILE560 |
B | GLU573 |
B | THR575 |
B | ILE587 |
B | PHE649 |
B | LEU650 |
B | TYR669 |
B | GLU676 |
B | TYR678 |
B | PHE717 |
B | TYR737 |
site_id | AC4 |
Number of Residues | 37 |
Details | binding site for FAD B 901 |
Chain | Residue |
B | GLY49 |
B | GLY51 |
B | CYS52 |
B | VAL53 |
B | LEU72 |
B | GLU73 |
B | LYS74 |
B | GLY80 |
B | SER81 |
B | THR82 |
B | HIS84 |
B | ALA85 |
B | ALA86 |
B | GLY87 |
B | LEU88 |
B | PRO211 |
B | VAL212 |
B | ALA240 |
B | ALA241 |
B | GLY242 |
B | TRP244 |
B | HIS263 |
B | TYR265 |
B | GLY363 |
B | PRO364 |
B | ILE365 |
B | PHE390 |
B | TYR392 |
B | GLY393 |
B | ILE394 |
B | ILE395 |
B | HOH1008 |
B | HOH1017 |
B | HOH1037 |
B | HOH1048 |
B | HOH1086 |
B | HOH1093 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24858690, ECO:0007744|PDB:4P9S, ECO:0007744|PDB:4PAA, ECO:0007744|PDB:4PAB |
Chain | Residue | Details |
A | CYS52 | |
B | PHE390 | |
A | GLU73 | |
A | GLY80 | |
A | VAL212 | |
A | PHE390 | |
B | CYS52 | |
B | GLU73 | |
B | GLY80 | |
B | VAL212 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24858690, ECO:0007744|PDB:4P9S, ECO:0007744|PDB:4PAB |
Chain | Residue | Details |
A | TRP244 | |
B | TRP244 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24858690, ECO:0007744|PDB:4PAA, ECO:0007744|PDB:4PAB |
Chain | Residue | Details |
A | GLU573 | |
A | GLU676 | |
A | TYR737 | |
B | GLU573 | |
B | GLU676 | |
B | TYR737 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24858690, ECO:0007744|PDB:4PAA |
Chain | Residue | Details |
A | TYR669 | |
B | TYR669 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Tele-8alpha-FAD histidine => ECO:0000269|PubMed:24858690, ECO:0000269|PubMed:4055729, ECO:0007744|PDB:4P9S, ECO:0007744|PDB:4PAA, ECO:0007744|PDB:4PAB |
Chain | Residue | Details |
A | HIS84 | |
B | HIS84 |
site_id | SWS_FT_FI6 |
Number of Residues | 12 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBT9 |
Chain | Residue | Details |
A | LYS107 | |
B | LYS328 | |
B | LYS353 | |
B | LYS757 | |
A | LYS161 | |
A | LYS216 | |
A | LYS328 | |
A | LYS353 | |
A | LYS757 | |
B | LYS107 | |
B | LYS161 | |
B | LYS216 |
site_id | SWS_FT_FI7 |
Number of Residues | 12 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBT9 |
Chain | Residue | Details |
A | LYS141 | |
B | LYS516 | |
B | LYS648 | |
B | LYS786 | |
A | LYS427 | |
A | LYS469 | |
A | LYS516 | |
A | LYS648 | |
A | LYS786 | |
B | LYS141 | |
B | LYS427 | |
B | LYS469 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9DBT9 |
Chain | Residue | Details |
A | LYS310 | |
A | LYS312 | |
A | LYS788 | |
B | LYS310 | |
B | LYS312 | |
B | LYS788 |