3WG7
A 1.9 angstrom radiation damage free X-ray structure of large (420KDa) protein by femtosecond crystallography
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004129 | molecular_function | cytochrome-c oxidase activity |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0006119 | biological_process | oxidative phosphorylation |
A | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
A | 0009060 | biological_process | aerobic respiration |
A | 0015990 | biological_process | electron transport coupled proton transport |
A | 0016020 | cellular_component | membrane |
A | 0020037 | molecular_function | heme binding |
A | 0045277 | cellular_component | respiratory chain complex IV |
A | 0046872 | molecular_function | metal ion binding |
B | 0004129 | molecular_function | cytochrome-c oxidase activity |
B | 0005507 | molecular_function | copper ion binding |
B | 0005739 | cellular_component | mitochondrion |
B | 0005743 | cellular_component | mitochondrial inner membrane |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0022900 | biological_process | electron transport chain |
B | 0042773 | biological_process | ATP synthesis coupled electron transport |
B | 0045277 | cellular_component | respiratory chain complex IV |
B | 0046872 | molecular_function | metal ion binding |
B | 1902600 | biological_process | proton transmembrane transport |
C | 0004129 | molecular_function | cytochrome-c oxidase activity |
C | 0005739 | cellular_component | mitochondrion |
C | 0005743 | cellular_component | mitochondrial inner membrane |
C | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
C | 0008535 | biological_process | respiratory chain complex IV assembly |
C | 0009055 | molecular_function | electron transfer activity |
C | 0016020 | cellular_component | membrane |
C | 0019646 | biological_process | aerobic electron transport chain |
C | 0022904 | biological_process | respiratory electron transport chain |
C | 0045277 | cellular_component | respiratory chain complex IV |
C | 1902600 | biological_process | proton transmembrane transport |
D | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
D | 0045277 | cellular_component | respiratory chain complex IV |
E | 0005743 | cellular_component | mitochondrial inner membrane |
E | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
E | 0045277 | cellular_component | respiratory chain complex IV |
F | 0005740 | cellular_component | mitochondrial envelope |
F | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
F | 0045277 | cellular_component | respiratory chain complex IV |
G | 0005743 | cellular_component | mitochondrial inner membrane |
H | 0005739 | cellular_component | mitochondrion |
H | 0005743 | cellular_component | mitochondrial inner membrane |
H | 0006119 | biological_process | oxidative phosphorylation |
H | 0045277 | cellular_component | respiratory chain complex IV |
I | 0005739 | cellular_component | mitochondrion |
I | 0005743 | cellular_component | mitochondrial inner membrane |
I | 0006119 | biological_process | oxidative phosphorylation |
I | 0045277 | cellular_component | respiratory chain complex IV |
J | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
J | 0045277 | cellular_component | respiratory chain complex IV |
K | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
L | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
L | 0045277 | cellular_component | respiratory chain complex IV |
M | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
M | 0045277 | cellular_component | respiratory chain complex IV |
N | 0004129 | molecular_function | cytochrome-c oxidase activity |
N | 0005739 | cellular_component | mitochondrion |
N | 0005743 | cellular_component | mitochondrial inner membrane |
N | 0006119 | biological_process | oxidative phosphorylation |
N | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
N | 0009060 | biological_process | aerobic respiration |
N | 0015990 | biological_process | electron transport coupled proton transport |
N | 0016020 | cellular_component | membrane |
N | 0020037 | molecular_function | heme binding |
N | 0045277 | cellular_component | respiratory chain complex IV |
N | 0046872 | molecular_function | metal ion binding |
O | 0004129 | molecular_function | cytochrome-c oxidase activity |
O | 0005507 | molecular_function | copper ion binding |
O | 0005739 | cellular_component | mitochondrion |
O | 0005743 | cellular_component | mitochondrial inner membrane |
O | 0016020 | cellular_component | membrane |
O | 0016491 | molecular_function | oxidoreductase activity |
O | 0022900 | biological_process | electron transport chain |
O | 0042773 | biological_process | ATP synthesis coupled electron transport |
O | 0045277 | cellular_component | respiratory chain complex IV |
O | 0046872 | molecular_function | metal ion binding |
O | 1902600 | biological_process | proton transmembrane transport |
P | 0004129 | molecular_function | cytochrome-c oxidase activity |
P | 0005739 | cellular_component | mitochondrion |
P | 0005743 | cellular_component | mitochondrial inner membrane |
P | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
P | 0008535 | biological_process | respiratory chain complex IV assembly |
P | 0009055 | molecular_function | electron transfer activity |
P | 0016020 | cellular_component | membrane |
P | 0019646 | biological_process | aerobic electron transport chain |
P | 0022904 | biological_process | respiratory electron transport chain |
P | 0045277 | cellular_component | respiratory chain complex IV |
P | 1902600 | biological_process | proton transmembrane transport |
Q | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
Q | 0045277 | cellular_component | respiratory chain complex IV |
R | 0005743 | cellular_component | mitochondrial inner membrane |
R | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
R | 0045277 | cellular_component | respiratory chain complex IV |
S | 0005740 | cellular_component | mitochondrial envelope |
S | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
S | 0045277 | cellular_component | respiratory chain complex IV |
T | 0005743 | cellular_component | mitochondrial inner membrane |
U | 0005739 | cellular_component | mitochondrion |
U | 0005743 | cellular_component | mitochondrial inner membrane |
U | 0006119 | biological_process | oxidative phosphorylation |
U | 0045277 | cellular_component | respiratory chain complex IV |
V | 0005739 | cellular_component | mitochondrion |
V | 0005743 | cellular_component | mitochondrial inner membrane |
V | 0006119 | biological_process | oxidative phosphorylation |
V | 0045277 | cellular_component | respiratory chain complex IV |
W | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
W | 0045277 | cellular_component | respiratory chain complex IV |
X | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
Y | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
Y | 0045277 | cellular_component | respiratory chain complex IV |
Z | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
Z | 0045277 | cellular_component | respiratory chain complex IV |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE HEA A 601 |
Chain | Residue |
A | MET28 |
A | MET65 |
A | ILE66 |
A | VAL70 |
A | ILE73 |
A | GLY125 |
A | TRP126 |
A | TYR371 |
A | PHE377 |
A | HIS378 |
A | SER382 |
A | THR31 |
A | VAL386 |
A | MET390 |
A | PHE393 |
A | MET417 |
A | PHE425 |
A | GLN428 |
A | ARG438 |
A | ARG439 |
A | TYR440 |
A | SER458 |
A | SER34 |
A | VAL465 |
A | MET468 |
A | HOH704 |
A | HOH725 |
A | HOH732 |
A | ILE37 |
A | ARG38 |
A | TYR54 |
A | VAL58 |
A | HIS61 |
A | ALA62 |
site_id | AC2 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE HEA A 602 |
Chain | Residue |
A | TRP126 |
A | TRP236 |
A | VAL243 |
A | TYR244 |
A | HIS290 |
A | HIS291 |
A | THR309 |
A | ILE312 |
A | THR316 |
A | GLY317 |
A | GLY352 |
A | GLY355 |
A | ILE356 |
A | LEU358 |
A | ALA359 |
A | ASP364 |
A | HIS368 |
A | VAL373 |
A | HIS376 |
A | PHE377 |
A | VAL380 |
A | LEU381 |
A | ARG438 |
A | PER606 |
A | HOH705 |
A | HOH712 |
A | HOH723 |
A | HOH731 |
B | ILE34 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU A 603 |
Chain | Residue |
A | HIS240 |
A | HIS290 |
A | HIS291 |
A | PER606 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 604 |
Chain | Residue |
A | HIS368 |
A | ASP369 |
A | HOH722 |
B | GLU198 |
B | HOH410 |
B | HOH411 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 605 |
Chain | Residue |
A | GLU40 |
A | GLY45 |
A | SER441 |
A | HOH720 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PER A 606 |
Chain | Residue |
A | HIS240 |
A | VAL243 |
A | HIS291 |
A | HEA602 |
A | CU603 |
site_id | AC7 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PGV A 607 |
Chain | Residue |
A | PHE94 |
A | PRO95 |
A | ARG96 |
A | MET97 |
A | HOH776 |
C | HIS9 |
C | ALA24 |
C | ASN50 |
C | TRP57 |
C | TRP58 |
C | GLU64 |
C | HIS71 |
C | LEU79 |
C | GLY82 |
C | PEK302 |
C | PGV303 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PGV A 608 |
Chain | Residue |
A | THR408 |
A | HOH778 |
A | HOH931 |
D | PHE87 |
K | PHE9 |
K | HIS10 |
M | PRO12 |
M | LEU19 |
M | HOH2316 |
A | ASN406 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TGL B 301 |
Chain | Residue |
A | ASN422 |
A | PHE426 |
A | PHE430 |
A | LEU433 |
B | LEU7 |
B | LEU28 |
B | PHE32 |
B | SER35 |
B | LEU39 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CUA B 302 |
Chain | Residue |
B | HIS161 |
B | CYS196 |
B | GLU198 |
B | CYS200 |
B | HIS204 |
B | MET207 |
site_id | BC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE CHD B 303 |
Chain | Residue |
A | MET271 |
A | TRP275 |
B | GLN59 |
B | GLU62 |
B | THR63 |
B | THR66 |
B | HOH455 |
B | HOH508 |
P | PEK308 |
T | ARG14 |
T | ARG17 |
T | PHE21 |
T | GLY22 |
site_id | BC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PSC B 304 |
Chain | Residue |
A | PHE321 |
B | ILE41 |
B | HIS52 |
B | MET56 |
B | ASP57 |
B | GLU60 |
B | HOH576 |
E | HIS5 |
E | ASP8 |
E | PHE11 |
E | LEU41 |
E | HOH217 |
I | ARG10 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA C 301 |
Chain | Residue |
C | HIS148 |
C | HIS232 |
C | GLU236 |
C | HOH404 |
site_id | BC5 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PEK C 302 |
Chain | Residue |
A | VAL155 |
A | ALA203 |
A | PGV607 |
C | TYR181 |
C | TYR182 |
C | ALA184 |
C | PHE186 |
C | THR187 |
C | ILE188 |
C | PHE198 |
C | GLY202 |
C | PHE203 |
G | TRP62 |
G | THR68 |
G | PHE69 |
G | PHE70 |
G | HIS71 |
G | ASN76 |
G | HOH205 |
site_id | BC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE PGV C 303 |
Chain | Residue |
A | PGV607 |
C | MET54 |
C | VAL61 |
C | SER65 |
C | THR66 |
C | ILE210 |
C | PHE214 |
C | ARG221 |
C | HIS226 |
C | PHE227 |
C | HIS231 |
C | PHE233 |
C | GLY234 |
C | CDL304 |
C | HOH432 |
C | HOH447 |
C | HOH475 |
F | HOH207 |
site_id | BC7 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE CDL C 304 |
Chain | Residue |
C | THR48 |
C | MET51 |
C | LEU52 |
C | MET54 |
C | TYR55 |
C | TRP58 |
C | ARG59 |
C | ILE62 |
C | ARG63 |
C | PHE67 |
C | SER212 |
C | THR213 |
C | ILE216 |
C | PHE220 |
C | ARG221 |
C | LYS224 |
C | HIS226 |
C | PGV303 |
C | HOH421 |
C | HOH500 |
C | HOH513 |
C | HOH537 |
J | LYS8 |
J | LEU31 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CHD C 305 |
Chain | Residue |
C | ARG156 |
C | PHE164 |
C | PHE219 |
C | LEU223 |
C | HOH510 |
J | PHE1 |
site_id | BC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CHD C 306 |
Chain | Residue |
A | HIS233 |
A | ASP300 |
A | THR301 |
A | TYR304 |
C | TRP99 |
C | HIS103 |
C | PGV308 |
C | HOH503 |
C | HOH535 |
P | LEU127 |
site_id | CC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PEK C 307 |
Chain | Residue |
C | LYS157 |
C | HIS158 |
C | GLN161 |
C | HOH525 |
G | ARG17 |
G | GLY22 |
G | CDL101 |
G | CHD103 |
G | HOH231 |
N | SER279 |
N | ILE311 |
O | GLN59 |
O | HOH486 |
site_id | CC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PGV C 308 |
Chain | Residue |
A | PHE237 |
C | THR95 |
C | TRP99 |
C | TYR102 |
C | HIS103 |
C | ALA107 |
C | CHD306 |
C | HOH523 |
C | HOH538 |
H | ASN24 |
T | ALA1 |
site_id | CC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE TGL D 201 |
Chain | Residue |
A | TRP334 |
A | LEU342 |
A | GLY343 |
A | ALA415 |
A | PHE418 |
A | VAL419 |
A | HOH908 |
B | LEU46 |
B | THR47 |
B | LYS49 |
B | HOH452 |
D | ARG73 |
D | SER74 |
D | THR75 |
D | GLU77 |
D | TRP78 |
D | HOH401 |
I | ARG16 |
I | HIS20 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN F 101 |
Chain | Residue |
F | CYS60 |
F | CYS62 |
F | CYS82 |
F | CYS85 |
site_id | CC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE CDL G 101 |
Chain | Residue |
C | LEU127 |
C | LEU131 |
C | LEU138 |
C | VAL254 |
C | PEK307 |
C | HOH528 |
G | SER27 |
G | LEU30 |
G | ASN34 |
G | LEU37 |
G | HIS38 |
G | HOH231 |
G | HOH241 |
G | HOH265 |
N | PHE282 |
N | ILE286 |
N | ASP300 |
N | SER307 |
N | ILE311 |
N | ILE314 |
O | ALA70 |
O | LEU78 |
O | LEU81 |
O | TYR85 |
site_id | CC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PEK G 102 |
Chain | Residue |
G | SER2 |
G | LYS5 |
G | GLY6 |
G | HOH236 |
G | HOH266 |
P | LYS77 |
P | ARG80 |
P | TYR81 |
P | VAL91 |
P | THR95 |
P | PHE98 |
P | TRP240 |
P | VAL247 |
site_id | CC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CHD G 103 |
Chain | Residue |
C | PEK307 |
G | ARG14 |
G | ARG17 |
G | PHE21 |
G | GLY22 |
G | HOH211 |
G | HOH228 |
G | HOH263 |
N | MET271 |
N | TRP275 |
O | GLU62 |
O | THR63 |
site_id | CC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CHD J 101 |
Chain | Residue |
A | ILE3 |
J | TYR32 |
J | ARG33 |
J | MET36 |
J | THR37 |
site_id | CC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE TGL L 101 |
Chain | Residue |
A | THR17 |
A | PHE22 |
A | TRP25 |
A | PHE400 |
A | SER401 |
L | PRO12 |
L | PHE13 |
L | SER14 |
L | ARG20 |
L | MET24 |
L | PHE28 |
L | PHE29 |
L | SER31 |
site_id | DC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMU M 101 |
Chain | Residue |
D | TRP98 |
M | LEU28 |
M | TRP32 |
M | TYR35 |
M | HIS36 |
M | HOH2331 |
site_id | DC2 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE HEA N 601 |
Chain | Residue |
N | GLY27 |
N | MET28 |
N | THR31 |
N | SER34 |
N | ILE37 |
N | ARG38 |
N | TYR54 |
N | VAL58 |
N | HIS61 |
N | ALA62 |
N | MET65 |
N | ILE66 |
N | VAL70 |
N | GLY125 |
N | TRP126 |
N | TYR371 |
N | PHE377 |
N | HIS378 |
N | SER382 |
N | VAL386 |
N | PHE393 |
N | PHE425 |
N | GLN428 |
N | ARG438 |
N | ARG439 |
N | MET468 |
N | HOH704 |
N | HOH724 |
N | HOH731 |
N | HOH911 |
Y | TGL101 |
site_id | DC3 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE HEA N 602 |
Chain | Residue |
N | TRP126 |
N | TRP236 |
N | VAL243 |
N | TYR244 |
N | HIS290 |
N | HIS291 |
N | THR309 |
N | ILE312 |
N | THR316 |
N | GLY317 |
N | GLY352 |
N | GLY355 |
N | ILE356 |
N | LEU358 |
N | ALA359 |
N | ASP364 |
N | HIS368 |
N | VAL373 |
N | HIS376 |
N | PHE377 |
N | VAL380 |
N | LEU381 |
N | ARG438 |
N | PER606 |
N | HOH705 |
N | HOH712 |
N | HOH722 |
N | HOH730 |
O | ILE34 |
site_id | DC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU N 603 |
Chain | Residue |
N | HIS240 |
N | HIS290 |
N | HIS291 |
N | PER606 |
site_id | DC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG N 604 |
Chain | Residue |
N | HIS368 |
N | ASP369 |
O | GLU198 |
O | HOH401 |
O | HOH411 |
O | HOH412 |
site_id | DC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA N 605 |
Chain | Residue |
N | GLU40 |
N | GLY45 |
N | SER441 |
N | HOH720 |
site_id | DC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PER N 606 |
Chain | Residue |
N | HIS240 |
N | VAL243 |
N | HIS291 |
N | HEA602 |
N | CU603 |
site_id | DC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PGV N 607 |
Chain | Residue |
N | ASN406 |
N | THR408 |
N | TRP409 |
Q | ALA84 |
Q | PHE87 |
X | PHE9 |
X | HIS10 |
Z | PRO12 |
Z | LEU19 |
Z | HOH222 |
Z | HOH223 |
site_id | DC9 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PGV N 608 |
Chain | Residue |
N | PHE94 |
N | PRO95 |
N | ARG96 |
N | MET97 |
N | HOH775 |
N | HOH791 |
P | HIS9 |
P | ASN50 |
P | MET54 |
P | TRP57 |
P | TRP58 |
P | GLU64 |
P | HIS71 |
P | SER89 |
P | PEK303 |
P | PGV304 |
P | HOH499 |
site_id | EC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE TGL N 609 |
Chain | Residue |
N | TYR379 |
N | ASN422 |
N | PHE426 |
N | LEU433 |
N | HOH899 |
N | HOH933 |
N | HOH940 |
O | LEU28 |
O | PHE32 |
O | SER35 |
O | LEU39 |
V | ARG43 |
V | HOH102 |
site_id | EC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PSC N 610 |
Chain | Residue |
N | PHE321 |
N | LEU324 |
N | HIS328 |
N | HOH913 |
N | HOH948 |
O | ILE41 |
O | HIS52 |
O | ASP57 |
R | HIS5 |
R | ASP8 |
R | PHE11 |
R | HOH204 |
R | HOH232 |
R | HOH294 |
V | ARG10 |
V | HOH101 |
site_id | EC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CUA O 301 |
Chain | Residue |
O | HIS161 |
O | CYS196 |
O | GLU198 |
O | CYS200 |
O | HIS204 |
O | MET207 |
site_id | EC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PGV P 301 |
Chain | Residue |
G | ALA1 |
N | HOH956 |
P | TYR102 |
P | HIS103 |
P | ALA107 |
P | CHD307 |
P | HOH512 |
U | ASN24 |
U | HOH123 |
site_id | EC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA P 302 |
Chain | Residue |
P | HIS148 |
P | HIS232 |
P | GLU236 |
site_id | EC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PEK P 303 |
Chain | Residue |
N | ALA203 |
N | PGV608 |
N | HOH953 |
P | TYR181 |
P | TYR182 |
P | ALA184 |
P | PHE186 |
P | THR187 |
P | ILE188 |
P | PHE198 |
P | HOH465 |
T | THR68 |
T | PHE69 |
T | PHE70 |
T | HIS71 |
T | ASN76 |
site_id | EC7 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE PGV P 304 |
Chain | Residue |
N | PGV608 |
P | MET54 |
P | TRP58 |
P | VAL61 |
P | SER65 |
P | THR66 |
P | ILE210 |
P | PHE214 |
P | ARG221 |
P | HIS226 |
P | PHE227 |
P | THR228 |
P | HIS231 |
P | PHE233 |
P | GLY234 |
P | CDL305 |
P | HOH429 |
P | HOH443 |
P | HOH475 |
P | HOH523 |
S | HOH208 |
site_id | EC8 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE CDL P 305 |
Chain | Residue |
P | THR48 |
P | MET51 |
P | LEU52 |
P | MET54 |
P | TYR55 |
P | TRP58 |
P | ARG59 |
P | ILE62 |
P | ARG63 |
P | PHE67 |
P | ILE216 |
P | VAL217 |
P | PHE220 |
P | LYS224 |
P | HIS226 |
P | PGV304 |
P | HOH417 |
P | HOH451 |
P | HOH498 |
W | LEU31 |
site_id | EC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CHD P 306 |
Chain | Residue |
P | ARG156 |
P | PHE164 |
P | PHE219 |
P | LEU223 |
W | PHE1 |
site_id | FC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CHD P 307 |
Chain | Residue |
C | LEU127 |
N | HIS233 |
N | ASP300 |
N | THR301 |
N | TYR304 |
P | TRP99 |
P | HIS103 |
P | PGV301 |
P | HOH492 |
site_id | FC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PEK P 308 |
Chain | Residue |
A | SER279 |
A | ILE311 |
B | CHD303 |
B | HOH582 |
P | LYS157 |
P | HIS158 |
P | GLN161 |
P | THR168 |
P | TYR172 |
P | HOH530 |
P | HOH539 |
S | ALA1 |
T | ARG17 |
T | GLY22 |
T | LEU25 |
T | CDL102 |
site_id | FC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE TGL Q 201 |
Chain | Residue |
N | TRP334 |
N | LEU342 |
N | GLY343 |
N | HOH890 |
O | LEU39 |
O | ILE42 |
O | THR47 |
O | THR48 |
O | HOH479 |
Q | ARG73 |
Q | GLU77 |
Q | TRP78 |
site_id | FC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN S 101 |
Chain | Residue |
S | CYS60 |
S | CYS62 |
S | CYS82 |
S | CYS85 |
site_id | FC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PEK T 101 |
Chain | Residue |
C | LYS77 |
C | ARG80 |
C | TYR81 |
C | ILE84 |
C | PHE98 |
C | TRP240 |
C | HOH529 |
C | HOH536 |
T | SER2 |
T | ALA3 |
T | LYS5 |
T | GLY6 |
T | HIS8 |
T | CDL102 |
site_id | FC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE CDL T 102 |
Chain | Residue |
A | ASP300 |
A | ALA303 |
A | SER307 |
A | ALA308 |
A | ILE311 |
A | ILE314 |
B | LEU81 |
B | ARG82 |
B | TYR85 |
P | LEU127 |
P | LEU131 |
P | PEK308 |
P | HOH515 |
P | HOH529 |
T | SER27 |
T | LEU30 |
T | CYS31 |
T | ASN34 |
T | LEU37 |
T | HIS38 |
T | PEK101 |
T | HOH222 |
T | HOH238 |
site_id | FC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CHD W 101 |
Chain | Residue |
W | TYR32 |
W | ARG33 |
W | MET36 |
W | THR37 |
W | HOH238 |
site_id | FC8 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE TGL Y 101 |
Chain | Residue |
N | PHE2 |
N | THR17 |
N | LEU18 |
N | PHE22 |
N | TRP25 |
N | LEU113 |
N | PHE400 |
N | SER401 |
N | HEA601 |
Y | ASN10 |
Y | ILE11 |
Y | PRO12 |
Y | PHE13 |
Y | ARG20 |
Y | MET24 |
Y | MET25 |
Y | PHE28 |
Y | SER31 |
Y | HOH235 |
site_id | FC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DMU Z 101 |
Chain | Residue |
N | PHE459 |
Q | TRP98 |
Z | LEU27 |
Z | LEU28 |
Z | TRP32 |
Z | TYR35 |
Z | HOH208 |
Z | HOH213 |
Functional Information from PROSITE/UniProt
site_id | PS00077 |
Number of Residues | 56 |
Details | COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwa.HH |
Chain | Residue | Details |
A | TRP236-HIS291 |
site_id | PS00078 |
Number of Residues | 49 |
Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavpslglktdaipgrlnqttlmssrpglyygq......CseiCgsnHsfM |
Chain | Residue | Details |
B | VAL159-MET207 |
site_id | PS00848 |
Number of Residues | 23 |
Details | COX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. VIWfwlhkgeaqrCpsCGthYKL |
Chain | Residue | Details |
F | VAL69-LEU91 |
site_id | PS01329 |
Number of Residues | 18 |
Details | COX6A Cytochrome c oxidase subunit VIa signature. IRtKpFsWGDGnHTfFhN |
Chain | Residue | Details |
G | ILE55-ASN72 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | TOPO_DOM: Mitochondrial matrix => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
M | ILE1-SER11 | |
N | SER262-GLY269 | |
N | SER401-ASN406 | |
N | LYS479-LYS514 | |
Z | ILE1-SER11 | |
F | CYS82 | |
F | CYS85 | |
S | CYS60 | |
S | CYS62 | |
S | CYS82 | |
S | CYS85 | |
N | MET171-PRO182 |
site_id | SWS_FT_FI2 |
Number of Residues | 46 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
M | PRO12-TYR35 | |
Z | PRO12-TYR35 | |
F | LYS90 | |
S | LYS37 | |
S | LYS55 | |
S | LYS90 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | TOPO_DOM: Mitochondrial intermembrane => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
M | HIS36-ALA46 | |
Z | HIS36-ALA46 | |
C | ALA184-ASP190 | |
C | TYR257-SER261 | |
P | PHE35-MET40 | |
P | LEU106-GLU128 | |
P | ALA184-ASP190 | |
P | TYR257-SER261 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17665 |
Chain | Residue | Details |
L | LYS9 | |
Y | LYS9 | |
Q | LYS7 | |
Q | LYS38 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P13073 |
Chain | Residue | Details |
D | LYS31 | |
O | CYS200 | |
O | HIS204 | |
O | MET207 | |
Q | LYS31 | |
B | GLU198 | |
B | CYS200 | |
B | HIS204 | |
B | MET207 | |
O | HIS161 | |
O | CYS196 | |
O | GLU198 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P10888 |
Chain | Residue | Details |
D | SER34 | |
D | SER36 | |
Q | SER34 | |
Q | SER36 | |
N | ARG213-ASP227 | |
N | VAL287-ASP298 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P19783 |
Chain | Residue | Details |
D | LYS45 | |
Q | LYS45 |
site_id | SWS_FT_FI8 |
Number of Residues | 64 |
Details | TRANSMEM: Helical; Name=VI => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
C | GLY191-LEU223 | |
P | GLY191-LEU223 |
site_id | SWS_FT_FI9 |
Number of Residues | 46 |
Details | TRANSMEM: Helical; Name=VII => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
C | PHE233-ILE256 | |
P | PHE233-ILE256 |
site_id | SWS_FT_FI10 |
Number of Residues | 32 |
Details | TRANSMEM: Helical; Name=VII => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
A | TYR270-ILE286 | |
N | TYR270-ILE286 |
site_id | SWS_FT_FI11 |
Number of Residues | 56 |
Details | TRANSMEM: Helical; Name=VIII => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
A | VAL299-LEU327 | |
N | VAL299-LEU327 |
site_id | SWS_FT_FI12 |
Number of Residues | 14 |
Details | TOPO_DOM: Mitochondrial matrix => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
A | HIS328-SER335 | |
N | HIS328-SER335 |
site_id | SWS_FT_FI13 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=IX => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
A | PRO336-VAL357 | |
N | PRO336-VAL357 |
site_id | SWS_FT_FI14 |
Number of Residues | 48 |
Details | TOPO_DOM: Mitochondrial intermembrane => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
A | LEU358-THR370 | |
A | SER434-ALA446 | |
N | LEU358-THR370 | |
N | SER434-ALA446 |
site_id | SWS_FT_FI15 |
Number of Residues | 58 |
Details | TRANSMEM: Helical; Name=X => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
A | TYR371-PHE400 | |
N | TYR371-PHE400 |
site_id | SWS_FT_FI16 |
Number of Residues | 52 |
Details | TRANSMEM: Helical; Name=XI => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
A | ASP407-LEU433 | |
N | ASP407-LEU433 |
site_id | SWS_FT_FI17 |
Number of Residues | 62 |
Details | TRANSMEM: Helical; Name=XII => ECO:0000269|PubMed:27605664 |
Chain | Residue | Details |
A | TYR447-SER478 | |
N | TYR447-SER478 |
site_id | SWS_FT_FI18 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27605664, ECO:0000305|PubMed:23537388 |
Chain | Residue | Details |
A | GLU40 | |
A | GLY45 | |
A | SER441 | |
N | GLU40 | |
N | GLY45 | |
N | SER441 |
site_id | SWS_FT_FI19 |
Number of Residues | 6 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158 |
Chain | Residue | Details |
A | HIS61 | |
A | HIS376 | |
A | HIS378 | |
N | HIS61 | |
N | HIS376 | |
N | HIS378 |
site_id | SWS_FT_FI20 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158 |
Chain | Residue | Details |
A | HIS240 | |
N | ASP369 | |
A | HIS290 | |
A | HIS291 | |
A | HIS368 | |
A | ASP369 | |
N | HIS240 | |
N | HIS290 | |
N | HIS291 | |
N | HIS368 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | TYR244 | |
N | TYR244 |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | MOD_RES: N-formylmethionine => ECO:0000269|PubMed:2165784 |
Chain | Residue | Details |
A | FME1 | |
N | FME1 |
site_id | SWS_FT_FI23 |
Number of Residues | 4 |
Details | CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr) => ECO:0000269|PubMed:10338009 |
Chain | Residue | Details |
A | HIS240 | |
A | TYR244 | |
N | HIS240 | |
N | TYR244 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 14 |
Details | M-CSA 124 |
Chain | Residue | Details |
A | HIS61 | metal ligand |
A | HIS290 | metal ligand |
A | HIS291 | metal ligand, proton acceptor, proton donor |
A | THR316 | proton acceptor, proton donor, proton relay |
A | LYS319 | proton acceptor, proton donor, proton relay |
A | ARG438 | proton acceptor, proton donor, proton relay |
A | ASP91 | proton acceptor, proton donor, proton relay |
A | TRP126 | proton acceptor, proton donor, proton relay |
A | SER156 | proton acceptor, proton donor, proton relay |
A | SER157 | proton acceptor, proton donor, proton relay |
A | HIS240 | covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser |
A | GLU242 | proton acceptor, proton donor, proton relay |
A | TYR244 | covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor |
A | SER255 | proton acceptor, proton donor, proton relay |
site_id | MCSA2 |
Number of Residues | 14 |
Details | M-CSA 124 |
Chain | Residue | Details |
N | HIS61 | metal ligand |
N | HIS290 | metal ligand |
N | HIS291 | metal ligand, proton acceptor, proton donor |
N | THR316 | proton acceptor, proton donor, proton relay |
N | LYS319 | proton acceptor, proton donor, proton relay |
N | ARG438 | proton acceptor, proton donor, proton relay |
N | ASP91 | proton acceptor, proton donor, proton relay |
N | TRP126 | proton acceptor, proton donor, proton relay |
N | SER156 | proton acceptor, proton donor, proton relay |
N | SER157 | proton acceptor, proton donor, proton relay |
N | HIS240 | covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser |
N | GLU242 | proton acceptor, proton donor, proton relay |
N | TYR244 | covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor |
N | SER255 | proton acceptor, proton donor, proton relay |