6HWH
Structure of a functional obligate respiratory supercomplex from Mycobacterium smegmatis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0046872 | molecular_function | metal ion binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
A | 0070469 | cellular_component | respirasome |
b | 0008121 | molecular_function | ubiquinol-cytochrome-c reductase activity |
b | 0009055 | molecular_function | electron transfer activity |
b | 0016020 | cellular_component | membrane |
b | 0016491 | molecular_function | oxidoreductase activity |
b | 0022904 | biological_process | respiratory electron transport chain |
b | 1902600 | biological_process | proton transmembrane transport |
B | 0005886 | cellular_component | plasma membrane |
B | 0046872 | molecular_function | metal ion binding |
B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0070469 | cellular_component | respirasome |
i | 0005506 | molecular_function | iron ion binding |
i | 0009055 | molecular_function | electron transfer activity |
i | 0016020 | cellular_component | membrane |
i | 0020037 | molecular_function | heme binding |
j | 0005506 | molecular_function | iron ion binding |
j | 0009055 | molecular_function | electron transfer activity |
j | 0016020 | cellular_component | membrane |
j | 0020037 | molecular_function | heme binding |
K | 0005506 | molecular_function | iron ion binding |
K | 0009055 | molecular_function | electron transfer activity |
K | 0016020 | cellular_component | membrane |
K | 0020037 | molecular_function | heme binding |
L | 0004129 | molecular_function | cytochrome-c oxidase activity |
L | 0005507 | molecular_function | copper ion binding |
L | 0016020 | cellular_component | membrane |
L | 0016491 | molecular_function | oxidoreductase activity |
L | 0046872 | molecular_function | metal ion binding |
L | 1902600 | biological_process | proton transmembrane transport |
M | 0005506 | molecular_function | iron ion binding |
M | 0009055 | molecular_function | electron transfer activity |
M | 0016020 | cellular_component | membrane |
M | 0020037 | molecular_function | heme binding |
N | 0016020 | cellular_component | membrane |
P | 0004129 | molecular_function | cytochrome-c oxidase activity |
P | 0005507 | molecular_function | copper ion binding |
P | 0016020 | cellular_component | membrane |
P | 0016491 | molecular_function | oxidoreductase activity |
P | 0046872 | molecular_function | metal ion binding |
P | 1902600 | biological_process | proton transmembrane transport |
Q | 0004129 | molecular_function | cytochrome-c oxidase activity |
Q | 0005886 | cellular_component | plasma membrane |
Q | 0006119 | biological_process | oxidative phosphorylation |
Q | 0009060 | biological_process | aerobic respiration |
Q | 0015990 | biological_process | electron transport coupled proton transport |
Q | 0016020 | cellular_component | membrane |
Q | 0016491 | molecular_function | oxidoreductase activity |
Q | 0020037 | molecular_function | heme binding |
Q | 0046872 | molecular_function | metal ion binding |
Q | 0070469 | cellular_component | respirasome |
R | 0016020 | cellular_component | membrane |
S | 0004129 | molecular_function | cytochrome-c oxidase activity |
S | 0005886 | cellular_component | plasma membrane |
S | 0016020 | cellular_component | membrane |
S | 0016491 | molecular_function | oxidoreductase activity |
S | 0022900 | biological_process | electron transport chain |
S | 1902600 | biological_process | proton transmembrane transport |
V | 0004129 | molecular_function | cytochrome-c oxidase activity |
V | 0005886 | cellular_component | plasma membrane |
V | 0006119 | biological_process | oxidative phosphorylation |
V | 0009060 | biological_process | aerobic respiration |
V | 0015990 | biological_process | electron transport coupled proton transport |
V | 0016020 | cellular_component | membrane |
V | 0016491 | molecular_function | oxidoreductase activity |
V | 0020037 | molecular_function | heme binding |
V | 0046872 | molecular_function | metal ion binding |
V | 0070469 | cellular_component | respirasome |
W | 0004129 | molecular_function | cytochrome-c oxidase activity |
W | 0005886 | cellular_component | plasma membrane |
W | 0009055 | molecular_function | electron transfer activity |
W | 0016020 | cellular_component | membrane |
W | 0016491 | molecular_function | oxidoreductase activity |
W | 0019646 | biological_process | aerobic electron transport chain |
W | 0022904 | biological_process | respiratory electron transport chain |
W | 1902600 | biological_process | proton transmembrane transport |
X | 0004129 | molecular_function | cytochrome-c oxidase activity |
X | 0005886 | cellular_component | plasma membrane |
X | 0016020 | cellular_component | membrane |
X | 0016491 | molecular_function | oxidoreductase activity |
X | 0022900 | biological_process | electron transport chain |
X | 1902600 | biological_process | proton transmembrane transport |
Y | 0008121 | molecular_function | ubiquinol-cytochrome-c reductase activity |
Y | 0009055 | molecular_function | electron transfer activity |
Y | 0016020 | cellular_component | membrane |
Y | 0016491 | molecular_function | oxidoreductase activity |
Y | 0022904 | biological_process | respiratory electron transport chain |
Y | 1902600 | biological_process | proton transmembrane transport |
Z | 0004129 | molecular_function | cytochrome-c oxidase activity |
Z | 0005886 | cellular_component | plasma membrane |
Z | 0009055 | molecular_function | electron transfer activity |
Z | 0016020 | cellular_component | membrane |
Z | 0016491 | molecular_function | oxidoreductase activity |
Z | 0019646 | biological_process | aerobic electron transport chain |
Z | 0022904 | biological_process | respiratory electron transport chain |
Z | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue FES A 501 |
Chain | Residue |
A | CYS333 |
A | HIS335 |
A | LEU336 |
A | CYS338 |
A | CYS352 |
A | CYS354 |
A | HIS355 |
A | SER357 |
site_id | AC2 |
Number of Residues | 15 |
Details | binding site for residue CDL M 301 |
Chain | Residue |
M | GLY259 |
M | MET262 |
M | TRP263 |
M | ARG267 |
X | TRP91 |
X | ALA115 |
X | PHE120 |
X | THR123 |
X | TRP134 |
X | GLU137 |
b | ARG487 |
b | LYS490 |
b | PHE502 |
b | CDL604 |
M | ILE251 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue MQ9 M 302 |
Chain | Residue |
M | MET247 |
M | TRP250 |
b | MET121 |
b | LEU124 |
b | ALA125 |
b | PHE128 |
b | PHE303 |
b | VAL340 |
b | ALA380 |
b | ILE381 |
b | TYR384 |
b | CDL603 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue CU P 401 |
Chain | Residue |
P | CYS273 |
P | CYS277 |
P | HIS281 |
P | MET284 |
P | CU402 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue CU P 402 |
Chain | Residue |
P | HIS232 |
P | CYS273 |
P | CYS277 |
P | MET284 |
P | CU401 |
site_id | AC6 |
Number of Residues | 27 |
Details | binding site for residue HAS V 801 |
Chain | Residue |
P | SER53 |
P | ALA56 |
P | SER57 |
P | VAL60 |
P | VAL64 |
V | TRP260 |
V | VAL267 |
V | TYR268 |
V | ILE270 |
V | HIS313 |
V | HIS314 |
V | ILE333 |
V | THR337 |
V | GLY338 |
V | PHE369 |
V | GLY373 |
V | GLY376 |
V | VAL377 |
V | LEU379 |
V | ASP385 |
V | THR389 |
V | VAL394 |
V | HIS397 |
V | PHE398 |
V | VAL401 |
V | LEU402 |
V | ARG459 |
site_id | AC7 |
Number of Residues | 19 |
Details | binding site for residue HAS V 802 |
Chain | Residue |
V | PHE52 |
V | GLY56 |
V | LEU57 |
V | ARG63 |
V | TYR79 |
V | PHE83 |
V | HIS86 |
V | MET90 |
V | LEU91 |
V | TRP151 |
V | TYR392 |
V | PHE398 |
V | HIS399 |
V | LEU402 |
V | PHE403 |
V | PHE446 |
V | ARG459 |
V | ARG460 |
V | LEU484 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue CU V 803 |
Chain | Residue |
V | HIS264 |
V | HIS313 |
V | HIS314 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue HEC V 804 |
Chain | Residue |
i | ASP183 |
i | LEU184 |
i | ASN202 |
i | HEC301 |
V | MET161 |
V | HIS162 |
i | THR93 |
i | PHE158 |
i | GLY178 |
site_id | AD1 |
Number of Residues | 17 |
Details | binding site for residue CDL V 805 |
Chain | Residue |
V | PHE118 |
V | PRO119 |
V | ARG120 |
V | LEU121 |
X | PHE99 |
X | ALA102 |
X | LEU128 |
Z | MET24 |
Z | GLY28 |
Z | THR29 |
Z | TRP32 |
Z | GLU36 |
Z | LEU149 |
Z | GLY153 |
Z | ARG164 |
Z | VAL180 |
Z | TYR184 |
site_id | AD2 |
Number of Residues | 17 |
Details | binding site for residue HEM b 601 |
Chain | Residue |
b | PHE40 |
b | GLY43 |
b | GLU44 |
b | ALA46 |
b | LEU47 |
b | ILE120 |
b | HIS123 |
b | LEU124 |
b | ARG126 |
b | ILE127 |
b | ALA132 |
b | TRP141 |
b | GLY144 |
b | HIS226 |
b | VAL230 |
b | HIS235 |
b | THR236 |
site_id | AD3 |
Number of Residues | 16 |
Details | binding site for residue HEM b 602 |
Chain | Residue |
Y | LEU213 |
b | PHE50 |
b | LEU53 |
b | GLY57 |
b | LEU60 |
b | ARG106 |
b | HIS109 |
b | HIS110 |
b | ALA113 |
b | GLU154 |
b | GLY155 |
b | GLY158 |
b | TYR159 |
b | PRO162 |
b | HIS211 |
b | ILE212 |
site_id | AD4 |
Number of Residues | 17 |
Details | binding site for residue CDL b 603 |
Chain | Residue |
M | MET262 |
M | ARG267 |
M | MQ9302 |
b | TRP38 |
b | SER39 |
b | PHE129 |
b | ARG366 |
b | PRO367 |
b | ARG368 |
b | THR374 |
b | SER378 |
b | ILE381 |
b | PHE389 |
b | TRP429 |
b | ALA430 |
b | LEU433 |
b | CDL604 |
site_id | AD5 |
Number of Residues | 15 |
Details | binding site for residue CDL b 604 |
Chain | Residue |
M | CDL301 |
V | TYR29 |
X | TRP90 |
X | TRP91 |
X | SER98 |
X | PHE120 |
b | ARG366 |
b | ARG368 |
b | TRP429 |
b | LEU433 |
b | PRO483 |
b | LYS486 |
b | ARG487 |
b | LYS490 |
b | CDL603 |
site_id | AD6 |
Number of Residues | 11 |
Details | binding site for residue MQ9 b 605 |
Chain | Residue |
Y | HIS21 |
Y | MQ9605 |
b | ARG28 |
b | GLN29 |
b | GLU44 |
b | GLY224 |
b | LEU227 |
b | ALA228 |
b | TRP231 |
b | PHE232 |
b | PHE257 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue FES B 501 |
Chain | Residue |
B | CYS333 |
B | HIS335 |
B | CYS338 |
B | CYS352 |
B | CYS354 |
B | HIS355 |
B | SER357 |
site_id | AD8 |
Number of Residues | 12 |
Details | binding site for residue CDL K 301 |
Chain | Residue |
K | ILE251 |
K | GLY259 |
K | MET262 |
K | TRP263 |
K | ARG267 |
S | PHE120 |
S | THR123 |
S | TRP134 |
S | GLU137 |
Y | ARG487 |
Y | LYS490 |
Y | CDL603 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue CU L 401 |
Chain | Residue |
L | CYS273 |
L | CYS277 |
L | HIS281 |
L | MET284 |
L | CU402 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue CU L 402 |
Chain | Residue |
L | HIS232 |
L | CYS273 |
L | CYS277 |
L | MET284 |
L | CU401 |
site_id | AE2 |
Number of Residues | 26 |
Details | binding site for residue HAS Q 801 |
Chain | Residue |
L | ALA56 |
L | SER57 |
L | VAL60 |
Q | TRP260 |
Q | VAL267 |
Q | TYR268 |
Q | ILE270 |
Q | HIS313 |
Q | HIS314 |
Q | ILE333 |
Q | THR337 |
Q | GLY338 |
Q | PHE369 |
Q | GLY373 |
Q | GLY376 |
Q | VAL377 |
Q | LEU379 |
Q | ALA380 |
Q | ASP385 |
Q | THR389 |
Q | VAL394 |
Q | HIS397 |
Q | PHE398 |
Q | VAL401 |
Q | LEU402 |
Q | ARG459 |
site_id | AE3 |
Number of Residues | 21 |
Details | binding site for residue HAS Q 802 |
Chain | Residue |
Q | PHE52 |
Q | GLY56 |
Q | LEU62 |
Q | ARG63 |
Q | TYR79 |
Q | PHE83 |
Q | HIS86 |
Q | GLY87 |
Q | MET90 |
Q | LEU91 |
Q | TRP151 |
Q | TYR392 |
Q | PHE398 |
Q | HIS399 |
Q | PHE403 |
Q | PHE446 |
Q | ARG459 |
Q | ARG460 |
Q | SER481 |
Q | LEU484 |
Q | GLY485 |
site_id | AE4 |
Number of Residues | 3 |
Details | binding site for residue CU Q 803 |
Chain | Residue |
Q | HIS264 |
Q | HIS313 |
Q | HIS314 |
site_id | AE5 |
Number of Residues | 17 |
Details | binding site for residue CDL Q 804 |
Chain | Residue |
Q | PHE118 |
Q | PRO119 |
Q | ARG120 |
Q | LEU121 |
S | PHE99 |
S | LEU128 |
S | VAL129 |
W | VAL25 |
W | THR29 |
W | TRP32 |
W | GLU36 |
W | LEU149 |
W | GLY153 |
W | ARG164 |
W | VAL180 |
W | VAL181 |
W | TYR184 |
site_id | AE6 |
Number of Residues | 19 |
Details | binding site for residue HEM Y 601 |
Chain | Residue |
Y | PHE50 |
Y | LEU53 |
Y | GLY57 |
Y | VAL58 |
Y | LEU60 |
Y | THR61 |
Y | ARG106 |
Y | HIS109 |
Y | HIS110 |
Y | ALA113 |
Y | GLU154 |
Y | GLY158 |
Y | TYR159 |
Y | PRO162 |
Y | HIS211 |
Y | ILE212 |
Y | PRO216 |
Y | ASN282 |
b | LEU213 |
site_id | AE7 |
Number of Residues | 20 |
Details | binding site for residue HEM Y 602 |
Chain | Residue |
Y | PHE40 |
Y | GLY43 |
Y | ALA46 |
Y | LEU47 |
Y | ILE120 |
Y | HIS123 |
Y | LEU124 |
Y | ARG126 |
Y | ILE127 |
Y | ALA132 |
Y | ARG137 |
Y | TRP141 |
Y | GLY144 |
Y | SER145 |
Y | ILE223 |
Y | HIS226 |
Y | VAL230 |
Y | HIS235 |
Y | THR236 |
Y | MQ9605 |
site_id | AE8 |
Number of Residues | 14 |
Details | binding site for residue CDL Y 603 |
Chain | Residue |
K | CDL301 |
Q | TYR29 |
Q | PHE131 |
S | TRP90 |
S | ILE93 |
S | SER98 |
Y | ARG366 |
Y | ARG368 |
Y | TRP429 |
Y | LEU433 |
Y | LEU484 |
Y | LYS486 |
Y | ARG487 |
Y | CDL604 |
site_id | AE9 |
Number of Residues | 16 |
Details | binding site for residue CDL Y 604 |
Chain | Residue |
K | MET262 |
K | ARG267 |
K | ALA268 |
Y | HIS37 |
Y | TRP38 |
Y | ALA125 |
Y | PHE129 |
Y | ARG366 |
Y | PRO367 |
Y | ARG368 |
Y | THR374 |
Y | TRP429 |
Y | ALA430 |
Y | LEU433 |
Y | CDL603 |
Y | MQ9606 |
site_id | AF1 |
Number of Residues | 11 |
Details | binding site for residue MQ9 Y 605 |
Chain | Residue |
Y | ALA25 |
Y | ARG28 |
Y | GLN29 |
Y | GLU44 |
Y | LEU227 |
Y | TRP231 |
Y | PHE232 |
Y | HEM602 |
b | HIS21 |
b | ARG28 |
b | MQ9605 |
site_id | AF2 |
Number of Residues | 16 |
Details | binding site for residue MQ9 Y 606 |
Chain | Residue |
K | MET247 |
K | TRP250 |
K | ILE258 |
Y | MET121 |
Y | LEU124 |
Y | ALA125 |
Y | PHE128 |
Y | PHE303 |
Y | TRP307 |
Y | VAL340 |
Y | LEU343 |
Y | TYR347 |
Y | ALA380 |
Y | ILE381 |
Y | TYR384 |
Y | CDL604 |
site_id | AF3 |
Number of Residues | 11 |
Details | binding site for residue HEC i 301 |
Chain | Residue |
A | SER341 |
A | LEU342 |
A | TYR343 |
V | HEC804 |
i | SER60 |
i | ALA86 |
i | VAL87 |
i | THR93 |
i | ARG95 |
i | MET96 |
i | GLN201 |
site_id | AF4 |
Number of Residues | 11 |
Details | binding site for residue HEC j 302 |
Chain | Residue |
j | SER92 |
j | THR93 |
j | GLY94 |
j | ASN161 |
j | CYS162 |
j | GLY178 |
j | ASP183 |
j | LEU184 |
j | ASN202 |
j | MET203 |
j | HEC301 |
site_id | AF5 |
Number of Residues | 17 |
Details | binding site for Ligand residues ARG A 243 through LYS A 255 bound to SER i 107 |
Chain | Residue |
A | GLN102 |
A | GLU107 |
A | GLU109 |
A | PHE110 |
A | LEU111 |
A | TYR112 |
A | TYR240 |
A | ALA242 |
A | ALA244 |
A | PHE253 |
A | VAL254 |
A | MET256 |
A | ASP260 |
A | TYR388 |
i | SER107 |
i | PRO109 |
i | PRO110 |
site_id | AF6 |
Number of Residues | 6 |
Details | binding site for Ligand ASP P 229 bound to SER i 164 |
Chain | Residue |
P | GLN137 |
P | ALA228 |
P | VAL230 |
i | ALA163 |
i | SER164 |
i | CYS165 |
site_id | AF7 |
Number of Residues | 15 |
Details | binding site for Di-peptide HIS Q 264 and TYR Q 268 |
Chain | Residue |
Q | TRP260 |
Q | PHE262 |
Q | GLY263 |
Q | PRO265 |
Q | GLU266 |
Q | VAL267 |
Q | ILE269 |
Q | ILE270 |
Q | LEU272 |
Q | SER307 |
Q | VAL310 |
Q | HIS314 |
Q | ILE333 |
Q | HAS801 |
Q | CU803 |
site_id | AF8 |
Number of Residues | 10 |
Details | binding site for Di-peptide HEC j 301 and THR j 93 |
Chain | Residue |
j | SER60 |
j | ALA86 |
j | VAL87 |
j | VAL91 |
j | SER92 |
j | GLY94 |
j | ARG95 |
j | MET96 |
j | GLN201 |
j | HEC302 |
site_id | AF9 |
Number of Residues | 10 |
Details | binding site for Di-peptide HEC j 301 and THR j 93 |
Chain | Residue |
j | SER60 |
j | ALA86 |
j | VAL87 |
j | VAL91 |
j | SER92 |
j | GLY94 |
j | ARG95 |
j | MET96 |
j | GLN201 |
j | HEC302 |
site_id | AG1 |
Number of Residues | 10 |
Details | binding site for Di-peptide HEC j 301 and THR j 93 |
Chain | Residue |
j | SER60 |
j | ALA86 |
j | VAL87 |
j | VAL91 |
j | SER92 |
j | GLY94 |
j | ARG95 |
j | MET96 |
j | GLN201 |
j | HEC302 |
Functional Information from PROSITE/UniProt
site_id | PS00077 |
Number of Residues | 55 |
Details | COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyiialpffgivteifpvfsrkpvfgyttlvyatisigalsiavwa..HH |
Chain | Residue | Details |
V | TRP260-HIS314 |
site_id | PS00078 |
Number of Residues | 55 |
Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHgfwvpeflfkrdvlpepkannsdnvfqvseiqqtgafvgrCtemCgtfHamM |
Chain | Residue | Details |
P | VAL230-MET284 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | CROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) => ECO:0000269|PubMed:20094657 |
Chain | Residue | Details |
T | LYS115 | |
O | LYS115 |