1KYO: PDB entry 1KYO
Yeast cytochrome BC1 complex with bound substrate cytochrome C. Determined by X-ray diffraction at 2.97 Å resolution. Released 6 Mar 2002.
- Method
- X-ray diffraction
- Resolution
- 2.97 Å
- Organisms
- Saccharomyces cerevisiae, Mus musculus
- Chains
- 23
- Atoms
- 35,643
- Mol. weight
- 507.23 kDa
- Ligands
- FES, SMA, HEC
- Released
- 6 Mar 2002
Explore 1KYO in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1KYO contains 216 α-helices and 165 β-strands across 23 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 23 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 30-33 | 4 | 1 |
| β-strand | 37-42 | 6 | 1 |
| β-strand | 48-54 | 7 | 1 |
| α-helix | 58-60 | 3 | |
| α-helix | 68-76 | 9 | |
| α-helix | 79-88 | 10 | |
| β-strand | 91-96 | 6 | 1 |
| β-strand | 101-107 | 7 | 1 |
| α-helix | 112-120 | 9 | |
| α-helix | 121-125 | 5 | |
| α-helix | 136-142 | 7 | |
| α-helix | 144-153 | 10 | |
| α-helix | 155-167 | 13 | |
| α-helix | 172-174 | 3 | |
| α-helix | 181-186 | 6 | |
| α-helix | 189-199 | 11 | |
| β-strand | 205-211 | 7 | 1 |
| α-helix | 215-224 | 10 | |
| β-strand | 246-251 | 6 | 2 |
| β-strand | 252 | 1 | 3 |
| β-strand | 258-265 | 8 | 2 |
| α-helix | 267-268 | 2 | |
| α-helix | 274-284 | 11 | |
| β-strand | 286-288 | 3 | 2 |
| α-helix | 292-295 | 4 | |
| α-helix | 301-306 | 6 | |
| β-strand | 313-320 | 8 | 2 |
| β-strand | 325-333 | 9 | 2 |
| α-helix | 339-355 | 17 | |
| α-helix | 359-377 | 19 | |
| α-helix | 382-395 | 14 | |
| α-helix | 402-410 | 9 | |
| α-helix | 414-424 | 11 | |
| β-strand | 431-436 | 6 | 2 |
| α-helix | 442-443 | 2 | |
| α-helix | 444-449 | 6 | |
Chain B: 16 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-20 | 3 | 4 |
| β-strand | 29-35 | 7 | 4 |
| α-helix | 47-54 | 8 | |
| β-strand | 59 | 1 | 5 |
| β-strand | 62 | 1 | 5 |
| α-helix | 64-74 | 11 | |
| β-strand | 79-82 | 4 | 4 |
| β-strand | 87-93 | 7 | 4 |
| α-helix | 95-97 | 3 | |
| α-helix | 98-111 | 14 | |
| β-strand | 112 | 1 | 5 |
| α-helix | 116-118 | 3 | |
| α-helix | 119-123 | 5 | |
| α-helix | 124-134 | 11 | |
| α-helix | 138-150 | 13 | |
| α-helix | 169-179 | 11 | |
| α-helix | 182-184 | 3 | |
| β-strand | 185-190 | 6 | 4 |
| α-helix | 194-201 | 8 | |
| α-helix | 212-214 | 3 | |
| β-strand | 228-232 | 5 | 6 |
| β-strand | 238-245 | 8 | 6 |
| α-helix | 250-259 | 10 | |
| β-strand | 273-278 | 6 | 6 |
| β-strand | 283-290 | 8 | 6 |
| α-helix | 294-309 | 16 | |
| α-helix | 324-327 | 4 | |
| β-strand | 352-357 | 6 | 6 |
| α-helix | 359-361 | 3 | |
Chain C: 23 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-6 | 4 | |
| α-helix | 8-13 | 6 | |
| α-helix | 14-18 | 5 | |
| β-strand | 21-23 | 3 | 7 |
| α-helix | 28-31 | 4 | |
| α-helix | 32-51 | 20 | |
| α-helix | 61-70 | 10 | |
| α-helix | 75-102 | 28 | |
| α-helix | 111-135 | 25 | |
| β-strand | 137 | 1 | 8 |
| α-helix | 138-148 | 11 | |
| α-helix | 149-153 | 5 | |
| α-helix | 158-166 | 9 | |
| α-helix | 173-204 | 32 | |
| β-strand | 218-220 | 3 | 7 |
| α-helix | 225-246 | 22 | |
| α-helix | 254-257 | 4 | |
| β-strand | 259 | 1 | 8 |
| α-helix | 273-275 | 3 | |
| α-helix | 276-284 | 9 | |
| α-helix | 288-300 | 13 | |
| α-helix | 301-304 | 4 | |
| α-helix | 305-308 | 4 | |
| β-strand | 313 | 1 | 9 |
| α-helix | 320-341 | 22 | |
| α-helix | 346-361 | 16 | |
| α-helix | 362-366 | 5 | |
| α-helix | 367-380 | 14 | |
Chain D: 13 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 64-67 | 4 | |
| α-helix | 69-72 | 4 | |
| α-helix | 83-85 | 3 | |
| α-helix | 87-99 | 13 | |
| α-helix | 101-103 | 3 | |
| β-strand | 111 | 1 | 10 |
| α-helix | 112-115 | 4 | |
| β-strand | 116 | 1 | 11 |
| β-strand | 120 | 1 | 11 |
| α-helix | 122-129 | 8 | |
| β-strand | 133-136 | 4 | 12 |
| β-strand | 145-148 | 4 | 12 |
| β-strand | 154 | 1 | 10 |
| α-helix | 155-157 | 3 | |
| α-helix | 162-167 | 6 | |
| α-helix | 188-196 | 9 | |
| α-helix | 202-203 | 2 | |
| β-strand | 213-214 | 2 | 13 |
| β-strand | 222-223 | 2 | 13 |
| α-helix | 244-259 | 16 | |
| α-helix | 263-297 | 35 | |
| β-strand | 299-302 | 4 | 2 |
Chain E: 6 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 43 | 1 | 14 |
| α-helix | 52-79 | 28 | |
| α-helix | 86-88 | 3 | |
| β-strand | 94-97 | 4 | 15 |
| β-strand | 106-111 | 6 | 16 |
| β-strand | 114-120 | 7 | 16 |
| α-helix | 123-130 | 8 | |
| α-helix | 134-136 | 3 | |
| α-helix | 143-146 | 4 | |
| β-strand | 152-156 | 5 | 16 |
| α-helix | 166 | 1 | |
| β-strand | 167-170 | 4 | 17 |
| β-strand | 175-178 | 4 | 17 |
| β-strand | 183-185 | 3 | 17 |
| β-strand | 191 | 1 | 17 |
| β-strand | 201 | 1 | 16 |
| β-strand | 205-207 | 3 | 15 |
| β-strand | 211-214 | 4 | 15 |
Chain F: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 77-86 | 10 | |
| α-helix | 89-108 | 20 | |
| α-helix | 124-142 | 19 | |
| α-helix | 143-145 | 3 | |
Chain G: 9 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-17 | 13 | |
| α-helix | 19-36 | 18 | |
| α-helix | 38-41 | 4 | |
| α-helix | 45-48 | 4 | |
| β-strand | 49 | 1 | 9 |
| α-helix | 54-62 | 9 | |
| α-helix | 65-83 | 19 | |
| α-helix | 90-92 | 3 | |
| α-helix | 94-95 | 2 | |
| α-helix | 104-122 | 19 | |
Chain H: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 19-21 | 3 | |
| β-strand | 22 | 1 | 3 |
| β-strand | 24-29 | 6 | 2 |
| α-helix | 31-33 | 3 | |
| β-strand | 34 | 1 | 14 |
| α-helix | 56-80 | 25 | |
| α-helix | 86-92 | 7 | |
15 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Ubiquinol-cytochrome C reductase complex core protein I | A, L | protein | 430 | Saccharomyces cerevisiae | P07256 (AlphaFold model) |
| Ubiquinol-cytochrome C reductase complex core protein 2 | B, M | protein | 352 | Saccharomyces cerevisiae | P07257 (AlphaFold model) |
| Cytochrome B | C, N | protein | 385 | Saccharomyces cerevisiae | P00163 (AlphaFold model) |
| Cytochrome C1, heme protein | D, O | protein | 248 | Saccharomyces cerevisiae | P07143 (AlphaFold model) |
| Ubiquinol-cytochrome C reductase iron-sulfur subunit | E, P | protein | 185 | Saccharomyces cerevisiae | P08067 |
| Ubiquinol-cytochrome C reductase complex 17 kd protein | F, Q | protein | 74 | Saccharomyces cerevisiae | P00127 |
| Ubiquinol-cytochrome C reductase complex 14 kd protein | G, R | protein | 126 | Saccharomyces cerevisiae | P00128 |
| Ubiquinol-cytochrome C reductase complex ubiquinone-binding protein qp-C | H, S | protein | 93 | Saccharomyces cerevisiae | P08525 |
| Ubiquinol-cytochrome C reductase complex 7.3 kd protein | I, T | protein | 57 | Saccharomyces cerevisiae | P22289 |
| Heavy chain (VH) of fv-fragment | J, U | protein | 127 | Mus musculus | |
| Light chain (VL) of fv-fragment | K, V | protein | 107 | Mus musculus | |
| Cytochrome C, iso-1 | W | protein | 108 | Saccharomyces cerevisiae | P00044 |
Sequence of entity 1 (A, L), FASTA
>1KYO_1 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I (chains A, L)
AEVTQLSNGIVVATEHNPAHTASVGVVFGSGAANENPYNNGVSNLWKNIFLSKENSAVAA
KEGLALSSNISRDFQSYIVSSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLKQ
VQDFEDNDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLENLVVADLESFANNHFLNSNAV
VVGTGNIKHEDLVNSIESKNLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVEG
EPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNIQEYQLCDNFNHFSLSYKDSGL
WGFSTATRNVTMIDDLIHFTLKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVNDA
NLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRLWDQDIAIAGTGQIEGLLDYMR
IRSDMSMMRW
Sequence of entity 2 (B, M), FASTA
>1KYO_2 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2 (chains B, M)
LTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNFQNTNTRSALKLVRESELLGG
TFKSTLDREYITLKATFLKDDLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQ
CPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFADKVYTKENLEVSGENVVEAD
LKRFVDESLLSTLPAGKSLVSKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVL
ANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAVVSSNIKKIVADLKKGKDLSP
AINYTKLKNAVQNESVSSPIELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL
Sequence of entity 3 (C, N), FASTA
>1KYO_3 CYTOCHROME B (chains C, N)
MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIEL
AFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII
FTLTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFF
ALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL
ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIPDKLLGVITMFAAIL
VLLVLPFTDRSVVRGNTFKVLSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF
AYFLIIVPVISTIENVLFYIGRVNK
Sequence of entity 4 (D, O), FASTA
>1KYO_4 CYTOCHROME C1, HEME PROTEIN (chains D, O)
MTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVCAACHSLDRVAWRTLVGVSHT
NEEVRNMAEEFEYDDEPDEQGNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIV
KARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGGSIAMARVLFDDMVEYEDGTP
ATTSQMAKDVTTFLNWCAEPEHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFV
FNPPKPRK
Sequence of entity 5 (E, P), FASTA
>1KYO_5 UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT (chains E, P)
KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLA
MAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP
QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGD
KVIVG
Sequence of entity 6 (F, Q), FASTA
>1KYO_6 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 17 KD PROTEIN (chains F, Q)
DTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPGYADLEHKEDCVEEFFHLQHY
LDTATAPRLFDKLK
Sequence of entity 7 (G, R), FASTA
>1KYO_7 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KD PROTEIN (chains G, R)
PQSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLGLKFDDLIAEENPIMQTALR
RLPEDESYARAYRIIRAHQTELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELD
NIEVSK
Sequence of entity 8 (H, S), FASTA
>1KYO_8 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C (chains H, S)
GPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIFHNAVFNSFRRFKSQFLYVLI
PAGIYWYWWKNGNEYNEFLYSKAGREELERVNV
Sequence of entity 9 (I, T), FASTA
>1KYO_9 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.3 KD PROTEIN (chains I, T)
SFSSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENHNKGKLWKDVKAKIAA
Sequence of entity 10 (J, U), FASTA
>1KYO_10 HEAVY CHAIN (VH) OF FV-FRAGMENT (chains J, U)
EVKLQESGAGLVQPSQSLSLTCSVTGYSITSGYYWNWIRLFPGNKLEWVGYISNVGDNNY
NPSLKDRLSITRDTSKNQFFLKLNSVTTEDTATYYCARSEYYSVTGYAMDYWGQGTTVTV
SSAWRHP
Sequence of entity 11 (K, V), FASTA
>1KYO_11 LIGHT CHAIN (VL) OF FV-FRAGMENT (chains K, V)
DIELTQTPVSLAASLGDRVTISCRASQDINNFLNWYQQKPDGTIKLLIYYTSRLHAGVPS
RFSGSGSGTDYSLTISNLEPEDIATYFCQHHIKFPWTFGAGTKLEIK
Sequence of entity 12 (W), FASTA
>1KYO_12 CYTOCHROME C, ISO-1 (chains W)
TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKK
NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| FES | FE2/S2 (inorganic) cluster | Fe2 S2 | 2 |
| SMA | Stigmatellin a | C30 H42 O7 | 2 |
| HEC | Heme C | C34 H36 Fe N4 O4 | 7 |
Primary citation
Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c. Lange, C., Hunte, C. Proc Natl Acad Sci U S A (2002) 99:2800-2805. DOI 10.1073/pnas.052704699 · PubMed
Other PDB entries of the same protein (UniProt P07256 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3CX5 1.9 Å, Structure of complex III with bound cytochrome c in reduced state and definition of a…
- 1EZV 2.3 Å, Structure of the yeast cytochrome BC1 complex co-crystallized with an antibody fv-fragment
- 1KB9 2.3 Å, Yeast cytochrome BC1 complex
- 2IBZ 2.3 Å, Yeast Cytochrome BC1 Complex with Stigmatellin
- 8YIO 2.35 Å, Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in azoxystrobin-bound state
- 9ETZ 2.4 Å, III2IV respiratory supercomplex from Saccharomyces cerevisiae
- 8YHQ 2.42 Å, Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in pyraclostrobin-bound state
- 1P84 2.5 Å, HDBT inhibited Yeast Cytochrome bc1 Complex
- 3CXH 2.5 Å, Structure of yeast complex III with isoform-2 cytochrome c bound and definition of a…
- 8ZJC 2.5 Å, Cryo-EM structure of Saccharomyces cerevisiae bc1 complex
- 8ZMT 2.52 Å, Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in Metyltetraprole-bound state
- 9BPB 2.57 Å, Tethered respiratory III2IV2 supercomplex from Saccharomyces cerevisiae
Browse structure collections
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