6HWH
Structure of a functional obligate respiratory supercomplex from Mycobacterium smegmatis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| b | 0005886 | cellular_component | plasma membrane |
| b | 0008121 | molecular_function | quinol-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 | 0046872 | molecular_function | metal ion binding |
| b | 1902600 | biological_process | proton transmembrane transport |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0022904 | biological_process | respiratory electron transport chain |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| 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 | 0042773 | biological_process | ATP synthesis coupled electron transport |
| 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 |
| 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 | 0042773 | biological_process | ATP synthesis coupled electron transport |
| 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 | 0022904 | biological_process | respiratory electron transport chain |
| Q | 0046872 | molecular_function | metal ion binding |
| 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 | 0022904 | biological_process | respiratory electron transport chain |
| V | 0046872 | molecular_function | metal ion binding |
| W | 0004129 | molecular_function | cytochrome-c oxidase activity |
| W | 0005886 | cellular_component | plasma membrane |
| W | 0009055 | molecular_function | electron transfer activity |
| W | 0009060 | biological_process | aerobic respiration |
| 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 | 0005886 | cellular_component | plasma membrane |
| Y | 0008121 | molecular_function | quinol-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 | 0046872 | molecular_function | metal ion binding |
| 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 | 0009060 | biological_process | aerobic respiration |
| 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 | PS00078 |
| Number of Residues | 55 |
| Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHgfwvpeflfkrdvlpepkannsdnvfqvseiqqtgafvgrCtemCgtfHamM |
| Chain | Residue | Details |
| P | VAL230-MET284 |
| 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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)","evidences":[{"source":"PubMed","id":"20094657","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
