5YJX
Structure of the Ndi1 protein from Saccharomyces cerevisiae in complex with myxothiazol.
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 | 32 |
| Details | binding site for residue FAD A 601 |
| Chain | Residue |
| A | GLY60 |
| A | THR91 |
| A | PRO92 |
| A | LEU94 |
| A | GLU128 |
| A | ALA129 |
| A | ALA175 |
| A | VAL176 |
| A | GLY177 |
| A | LEU195 |
| A | ARG344 |
| A | SER61 |
| A | GLY382 |
| A | ASP383 |
| A | PRO391 |
| A | THR392 |
| A | ALA393 |
| A | GLN394 |
| A | TYR482 |
| A | MG602 |
| A | MG603 |
| A | MG604 |
| A | GLY62 |
| A | MG605 |
| A | MES606 |
| A | MYX607 |
| A | TRP63 |
| A | GLY64 |
| A | ILE82 |
| A | SER83 |
| A | PRO84 |
| A | ARG85 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue MG A 602 |
| Chain | Residue |
| A | ALA175 |
| A | VAL176 |
| A | GLY177 |
| A | ILE381 |
| A | GLY382 |
| A | ASP383 |
| A | ASN384 |
| A | FAD601 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 603 |
| Chain | Residue |
| A | GLY62 |
| A | TRP63 |
| A | GLY64 |
| A | ALA65 |
| A | ALA175 |
| A | FAD601 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 604 |
| Chain | Residue |
| A | GLY62 |
| A | TRP63 |
| A | ARG85 |
| A | LEU89 |
| A | THR91 |
| A | FAD601 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 605 |
| Chain | Residue |
| A | GLY177 |
| A | ALA178 |
| A | LYS196 |
| A | FAD601 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue MES A 606 |
| Chain | Residue |
| A | GLY237 |
| A | PRO238 |
| A | THR239 |
| A | THR339 |
| A | GLY340 |
| A | ASN341 |
| A | FAD601 |
| A | MYX607 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue MYX A 607 |
| Chain | Residue |
| A | TRP63 |
| A | PRO238 |
| A | MET280 |
| A | GLN394 |
| A | HIS397 |
| A | ALA446 |
| A | MET485 |
| A | FAD601 |
| A | MES606 |
| site_id | AC8 |
| Number of Residues | 29 |
| Details | binding site for residue FAD B 601 |
| Chain | Residue |
| B | MG604 |
| B | MG605 |
| B | MYX607 |
| B | GLY60 |
| B | SER61 |
| B | GLY62 |
| B | TRP63 |
| B | GLY64 |
| B | ILE82 |
| B | PRO84 |
| B | ARG85 |
| B | THR91 |
| B | PRO92 |
| B | GLU128 |
| B | ALA129 |
| B | ALA175 |
| B | VAL176 |
| B | GLY177 |
| B | LEU195 |
| B | THR239 |
| B | ARG344 |
| B | GLY382 |
| B | ASP383 |
| B | PRO391 |
| B | THR392 |
| B | ALA393 |
| B | TYR482 |
| B | MG602 |
| B | MG603 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 602 |
| Chain | Residue |
| B | ALA175 |
| B | GLY177 |
| B | ILE381 |
| B | GLY382 |
| B | ASP383 |
| B | ASN384 |
| B | FAD601 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 603 |
| Chain | Residue |
| B | GLY62 |
| B | GLY64 |
| B | ALA65 |
| B | ALA175 |
| B | FAD601 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 604 |
| Chain | Residue |
| B | GLY62 |
| B | TRP63 |
| B | ARG85 |
| B | LEU89 |
| B | THR91 |
| B | FAD601 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 605 |
| Chain | Residue |
| B | GLY177 |
| B | ALA178 |
| B | ASP383 |
| B | FAD601 |
| site_id | AD4 |
| Number of Residues | 10 |
| Details | binding site for residue MES B 606 |
| Chain | Residue |
| B | PRO180 |
| B | LEU195 |
| B | LYS196 |
| B | GLY237 |
| B | PRO238 |
| B | THR239 |
| B | ALA338 |
| B | GLY340 |
| B | ASN341 |
| B | MYX607 |
| site_id | AD5 |
| Number of Residues | 11 |
| Details | binding site for residue MYX B 607 |
| Chain | Residue |
| B | TRP63 |
| B | MET280 |
| B | ASN341 |
| B | PRO391 |
| B | THR392 |
| B | GLN394 |
| B | HIS397 |
| B | LEU447 |
| B | MET485 |
| B | FAD601 |
| B | MES606 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 132 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
