3RKO
Crystal structure of the membrane domain of respiratory complex I from E. coli at 3.0 angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| A | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| B | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| B | 0042773 | biological_process | ATP synthesis coupled electron transport |
| C | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| C | 0042773 | biological_process | ATP synthesis coupled electron transport |
| D | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| D | 0042773 | biological_process | ATP synthesis coupled electron transport |
| E | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| E | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| F | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| G | 0030964 | cellular_component | NADH dehydrogenase complex |
| G | 0042773 | biological_process | ATP synthesis coupled electron transport |
| G | 0048038 | molecular_function | quinone binding |
| G | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| J | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| K | 0005886 | cellular_component | plasma membrane |
| K | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| K | 0030964 | cellular_component | NADH dehydrogenase complex |
| K | 0042773 | biological_process | ATP synthesis coupled electron transport |
| K | 0048038 | molecular_function | quinone binding |
| K | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| L | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| L | 0042773 | biological_process | ATP synthesis coupled electron transport |
| M | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| M | 0042773 | biological_process | ATP synthesis coupled electron transport |
| N | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| N | 0042773 | biological_process | ATP synthesis coupled electron transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LFA L 614 |
| Chain | Residue |
| L | LYS169 |
| L | VAL173 |
| L | PHE549 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LFA L 615 |
| Chain | Residue |
| M | MET398 |
| M | PRO399 |
| M | LFA512 |
| L | ALA19 |
| L | ARG22 |
| L | TYR119 |
| L | LEU148 |
| M | ALA386 |
| M | LEU389 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LFA L 616 |
| Chain | Residue |
| L | SER90 |
| L | PHE340 |
| L | LEU463 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CA7 M 510 |
| Chain | Residue |
| L | MET168 |
| L | PHE549 |
| L | PHE553 |
| L | LEU554 |
| M | VAL434 |
| M | HIS441 |
| M | ARG442 |
| M | PHE445 |
| M | GLY446 |
| M | LYS447 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LFA M 511 |
| Chain | Residue |
| M | TYR221 |
| M | ALA232 |
| M | VAL237 |
| M | VAL238 |
| M | LEU240 |
| M | LEU293 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LFA M 512 |
| Chain | Residue |
| L | PHE20 |
| L | LFA615 |
| M | TRP383 |
| M | ALA386 |
| M | LEU387 |
| M | PHE480 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE LFA N 486 |
| Chain | Residue |
| N | TRP408 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LFA N 487 |
| Chain | Residue |
| N | VAL42 |
| N | ILE43 |
| N | ASN46 |
| N | TYR92 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LFA N 488 |
| Chain | Residue |
| N | MET74 |
| N | LEU75 |
| N | LEU480 |
| N | ALA481 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE LFA N 489 |
| Chain | Residue |
| N | TRP408 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LFA B 614 |
| Chain | Residue |
| B | LYS169 |
| B | VAL172 |
| B | VAL173 |
| B | LEU235 |
| B | PHE549 |
| B | VAL550 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LFA B 615 |
| Chain | Residue |
| B | ALA19 |
| B | ARG22 |
| B | TYR119 |
| B | LEU148 |
| C | ALA386 |
| C | LEU389 |
| C | MET398 |
| C | PRO399 |
| C | LFA513 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LFA B 616 |
| Chain | Residue |
| B | SER90 |
| B | PHE340 |
| B | LEU463 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CA7 C 510 |
| Chain | Residue |
| B | MET168 |
| B | PHE553 |
| B | LEU554 |
| C | VAL434 |
| C | HIS441 |
| C | ARG442 |
| C | PHE445 |
| C | GLY446 |
| C | LYS447 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LFA C 511 |
| Chain | Residue |
| C | TYR221 |
| C | ALA232 |
| C | VAL237 |
| C | VAL238 |
| C | LEU240 |
| C | LEU293 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LFA C 512 |
| Chain | Residue |
| C | LEU223 |
| D | TRP408 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LFA C 513 |
| Chain | Residue |
| B | PHE20 |
| B | LFA615 |
| C | TRP383 |
| C | ALA386 |
| C | LEU387 |
| C | PHE480 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LFA D 486 |
| Chain | Residue |
| D | VAL42 |
| D | ASN46 |
| D | CYS88 |
| D | THR89 |
| D | TYR92 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LFA D 487 |
| Chain | Residue |
| D | MET74 |
| D | LEU75 |
| D | ALA481 |
| site_id | CC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE LFA D 488 |
| Chain | Residue |
| D | TRP408 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 120 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01456","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






