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 | 0016020 | cellular_component | 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 | 0016020 | cellular_component | 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 |