4GAV
Structure of the Ndi1 protein from Saccharomyces cerevisiae in complex with quinone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003954 | molecular_function | NADH dehydrogenase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006120 | biological_process | mitochondrial electron transport, NADH to ubiquinone |
| A | 0015980 | biological_process | energy derivation by oxidation of organic compounds |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043065 | biological_process | positive regulation of apoptotic process |
| A | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| A | 0120555 | molecular_function | NADH dehydrogenase (ubiquinone) (non-electrogenic) activity |
| B | 0003954 | molecular_function | NADH dehydrogenase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006120 | biological_process | mitochondrial electron transport, NADH to ubiquinone |
| B | 0015980 | biological_process | energy derivation by oxidation of organic compounds |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043065 | biological_process | positive regulation of apoptotic process |
| B | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| B | 0120555 | molecular_function | NADH dehydrogenase (ubiquinone) (non-electrogenic) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD A 601 |
| Chain | Residue |
| A | GLY60 |
| A | THR91 |
| A | PRO92 |
| A | GLU128 |
| A | ALA129 |
| A | VAL176 |
| A | GLY177 |
| A | LEU195 |
| A | THR239 |
| A | ARG344 |
| A | VAL346 |
| A | SER61 |
| A | GLY382 |
| A | ASP383 |
| A | PRO391 |
| A | THR392 |
| A | ALA393 |
| A | GLN394 |
| A | TYR482 |
| A | UQ2602 |
| A | GLY62 |
| A | TRP63 |
| A | GLY64 |
| A | ILE82 |
| A | SER83 |
| A | PRO84 |
| A | ARG85 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE UQ2 A 602 |
| Chain | Residue |
| A | TRP63 |
| A | PRO238 |
| A | THR392 |
| A | ALA393 |
| A | GLN394 |
| A | GLY445 |
| A | LEU447 |
| A | TYR482 |
| A | MET485 |
| A | FAD601 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD B 601 |
| Chain | Residue |
| B | GLY60 |
| B | SER61 |
| B | GLY62 |
| B | TRP63 |
| B | GLY64 |
| B | SER83 |
| B | PRO84 |
| B | ARG85 |
| B | THR91 |
| B | PRO92 |
| B | ALA129 |
| B | ALA175 |
| B | VAL176 |
| B | GLY177 |
| B | LEU195 |
| B | THR239 |
| B | ARG344 |
| B | VAL346 |
| B | GLY382 |
| B | ASP383 |
| B | PRO391 |
| B | THR392 |
| B | ALA393 |
| B | TYR482 |
| B | UQ2602 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE UQ2 B 602 |
| Chain | Residue |
| B | TRP63 |
| B | PRO238 |
| B | THR392 |
| B | GLN394 |
| B | GLY445 |
| B | LEU447 |
| B | TYR482 |
| B | MET485 |
| B | FAD601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 132 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
