1DXL
Dihydrolipoamide dehydrogenase of glycine decarboxylase from Pisum Sativum
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005960 | cellular_component | glycine cleavage complex |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
A | 0045252 | cellular_component | oxoglutarate dehydrogenase complex |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0005960 | cellular_component | glycine cleavage complex |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
B | 0045252 | cellular_component | oxoglutarate dehydrogenase complex |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
C | 0005739 | cellular_component | mitochondrion |
C | 0005759 | cellular_component | mitochondrial matrix |
C | 0005960 | cellular_component | glycine cleavage complex |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
C | 0045252 | cellular_component | oxoglutarate dehydrogenase complex |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
D | 0005739 | cellular_component | mitochondrion |
D | 0005759 | cellular_component | mitochondrial matrix |
D | 0005960 | cellular_component | glycine cleavage complex |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
D | 0045252 | cellular_component | oxoglutarate dehydrogenase complex |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE FAD A 480 |
Chain | Residue |
A | ILE12 |
A | CYS45 |
A | VAL48 |
A | GLY49 |
A | CYS50 |
A | LYS54 |
A | GLY116 |
A | TYR117 |
A | GLY118 |
A | ALA146 |
A | THR147 |
A | GLY15 |
A | GLY148 |
A | SER149 |
A | SER167 |
A | TYR187 |
A | ILE188 |
A | ARG277 |
A | ASP317 |
A | MET323 |
A | LEU324 |
A | ALA325 |
A | PRO16 |
A | HIS326 |
A | ALA328 |
A | TYR356 |
B | HIS449 |
A | GLY17 |
A | GLU36 |
A | LYS37 |
A | ARG38 |
A | GLY43 |
A | THR44 |
site_id | AC2 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD B 480 |
Chain | Residue |
A | HIS449 |
B | ILE12 |
B | GLY15 |
B | PRO16 |
B | GLY17 |
B | ILE35 |
B | GLU36 |
B | LYS37 |
B | ARG38 |
B | GLY43 |
B | THR44 |
B | CYS45 |
B | GLY49 |
B | CYS50 |
B | LYS54 |
B | GLY116 |
B | TYR117 |
B | GLY118 |
B | ALA146 |
B | THR147 |
B | GLY148 |
B | SER149 |
B | ILE188 |
B | ARG277 |
B | LEU284 |
B | ASP317 |
B | MET323 |
B | LEU324 |
B | ALA325 |
B | HIS326 |
B | ALA328 |
B | HOH2006 |
site_id | AC3 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE FAD C 480 |
Chain | Residue |
C | ILE12 |
C | GLY13 |
C | GLY14 |
C | GLY15 |
C | PRO16 |
C | GLY17 |
C | GLU36 |
C | LYS37 |
C | ARG38 |
C | GLY43 |
C | THR44 |
C | CYS45 |
C | VAL48 |
C | GLY49 |
C | LYS54 |
C | GLY116 |
C | TYR117 |
C | GLY118 |
C | ALA146 |
C | THR147 |
C | GLY148 |
C | ILE188 |
C | ARG277 |
C | PHE280 |
C | ASP317 |
C | MET323 |
C | LEU324 |
C | ALA325 |
C | HIS326 |
C | ALA328 |
C | TYR356 |
C | HOH2001 |
D | HIS449 |
site_id | AC4 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD D 480 |
Chain | Residue |
D | ILE12 |
D | GLY14 |
D | GLY15 |
D | PRO16 |
D | GLY17 |
D | ILE35 |
D | GLU36 |
D | LYS37 |
D | ARG38 |
D | GLY43 |
D | THR44 |
D | CYS45 |
D | GLY49 |
D | CYS50 |
D | LYS54 |
D | GLY116 |
D | TYR117 |
D | GLY118 |
D | ALA146 |
D | THR147 |
D | GLY148 |
D | SER149 |
D | ILE188 |
D | ARG277 |
D | ASP317 |
D | MET323 |
D | LEU324 |
D | ALA325 |
D | HIS326 |
D | ALA328 |
D | TYR356 |
C | HIS449 |
Functional Information from PROSITE/UniProt
site_id | PS00076 |
Number of Residues | 11 |
Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCLnvGCIP |
Chain | Residue | Details |
A | GLY42-PRO52 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | HIS449 | |
B | HIS449 | |
C | HIS449 | |
D | HIS449 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10806386 |
Chain | Residue | Details |
A | GLU36 | |
C | GLY118 | |
C | ASP317 | |
C | MET323 | |
D | GLU36 | |
D | GLY118 | |
D | ASP317 | |
D | MET323 | |
A | GLY118 | |
A | ASP317 | |
A | MET323 | |
B | GLU36 | |
B | GLY118 | |
B | ASP317 | |
B | MET323 | |
C | GLU36 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | LYS54 | |
B | GLU207 | |
B | VAL241 | |
B | GLY276 | |
C | LYS54 | |
C | THR147 | |
C | GLY184 | |
C | GLU207 | |
C | VAL241 | |
C | GLY276 | |
D | LYS54 | |
A | THR147 | |
D | THR147 | |
D | GLY184 | |
D | GLU207 | |
D | VAL241 | |
D | GLY276 | |
A | GLY184 | |
A | GLU207 | |
A | VAL241 | |
A | GLY276 | |
B | LYS54 | |
B | THR147 | |
B | GLY184 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | GLU454 | |
A | HIS449 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
B | GLU454 | |
B | HIS449 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
C | GLU454 | |
C | HIS449 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
D | GLU454 | |
D | HIS449 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | CYS45 | |
A | CYS50 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
B | CYS45 | |
B | CYS50 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
C | CYS45 | |
C | CYS50 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
D | CYS45 | |
D | CYS50 |