4JDR
Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005960 | cellular_component | glycine cleavage complex |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015036 | molecular_function | disulfide oxidoreductase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| A | 0019464 | biological_process | glycine decarboxylation via glycine cleavage system |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042867 | biological_process | pyruvate catabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005960 | cellular_component | glycine cleavage complex |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0015036 | molecular_function | disulfide oxidoreductase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| B | 0019464 | biological_process | glycine decarboxylation via glycine cleavage system |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042867 | biological_process | pyruvate catabolic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD A 501 |
| Chain | Residue |
| A | GLY13 |
| A | VAL44 |
| A | CYS45 |
| A | GLY49 |
| A | CYS50 |
| A | LYS54 |
| A | GLY115 |
| A | LEU116 |
| A | GLY117 |
| A | ALA144 |
| A | ALA145 |
| A | ALA14 |
| A | GLY146 |
| A | ILE186 |
| A | ARG273 |
| A | LEU280 |
| A | GLY312 |
| A | ASP313 |
| A | MET319 |
| A | LEU320 |
| A | ALA321 |
| A | HIS322 |
| A | GLY15 |
| A | TYR352 |
| A | HOH601 |
| A | HOH616 |
| A | HOH639 |
| A | HOH648 |
| A | HOH649 |
| A | HOH650 |
| A | HOH779 |
| A | HOH828 |
| B | HIS445 |
| A | PRO16 |
| B | HOH720 |
| A | ALA17 |
| A | GLU36 |
| A | ARG37 |
| A | TYR38 |
| A | GLY43 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MES A 502 |
| Chain | Residue |
| A | ILE185 |
| A | ILE211 |
| A | PRO212 |
| A | ALA213 |
| A | GLN317 |
| A | PRO318 |
| A | LEU320 |
| A | MES503 |
| A | SO4504 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MES A 503 |
| Chain | Residue |
| A | GLY182 |
| A | GLY184 |
| A | VAL204 |
| A | GLU205 |
| A | MET206 |
| A | ILE271 |
| A | MES502 |
| A | SO4504 |
| A | HOH690 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 504 |
| Chain | Residue |
| A | ILE185 |
| A | ILE186 |
| A | MES502 |
| A | MES503 |
| A | HOH664 |
| A | HOH690 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 505 |
| Chain | Residue |
| A | ASP281 |
| A | ALA282 |
| A | GLY283 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 506 |
| Chain | Residue |
| A | ARG263 |
| A | HOH685 |
| A | HOH731 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 507 |
| Chain | Residue |
| A | ASP298 |
| A | LYS299 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 508 |
| Chain | Residue |
| A | TYR374 |
| A | GLU375 |
| A | THR376 |
| site_id | AC9 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD B 501 |
| Chain | Residue |
| B | LEU280 |
| B | GLY312 |
| B | ASP313 |
| B | MET319 |
| B | LEU320 |
| B | ALA321 |
| B | HIS322 |
| B | TYR352 |
| B | HOH603 |
| B | HOH614 |
| B | HOH625 |
| B | HOH643 |
| B | HOH658 |
| B | HOH714 |
| B | HOH718 |
| B | HOH760 |
| A | HIS445 |
| A | HOH711 |
| B | GLY13 |
| B | ALA14 |
| B | GLY15 |
| B | PRO16 |
| B | ALA17 |
| B | GLU36 |
| B | ARG37 |
| B | TYR38 |
| B | GLY43 |
| B | VAL44 |
| B | CYS45 |
| B | GLY49 |
| B | CYS50 |
| B | LYS54 |
| B | GLY115 |
| B | LEU116 |
| B | GLY117 |
| B | ALA144 |
| B | ALA145 |
| B | GLY146 |
| B | ILE186 |
| B | ARG273 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MES B 502 |
| Chain | Residue |
| B | GLY184 |
| B | ILE185 |
| B | ILE186 |
| B | PRO212 |
| B | ALA213 |
| B | HOH666 |
| B | HOH683 |
| B | HOH734 |
| B | HOH766 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 503 |
| Chain | Residue |
| B | ARG263 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 504 |
| Chain | Residue |
| B | GLY121 |
| B | ALA122 |
| B | ASN123 |
| B | THR124 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGvCLnvGCIP |
| Chain | Residue | Details |
| A | GLY42-PRO52 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
