4QLQ: YCP
yCP in complex with tripeptidic epoxyketone inhibitor 8. Determined by X-ray diffraction at 2.4 Å resolution. Released 23 Jul 2014.
- Method
- X-ray diffraction
- Resolution
- 2.4 Å
- Organism
- Saccharomyces cerevisiae
- Chains
- 28
- Atoms
- 50,332
- Mol. weight
- 734.38 kDa
- Ligands
- 38N, MG
- Released
- 23 Jul 2014
Explore 4QLQ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4QLQ contains 250 α-helices and 403 β-strands across 28 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.
Chains a and M: 7 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-8 | 3 | 9 |
| β-strand | 11-15 | 5 | 10 |
| β-strand | 19-25 | 7 | 10 |
| β-strand | 28-30 | 3 | 9 |
| β-strand | 33-36 | 4 | 9 |
| β-strand | 42-44 | 3 | 9 |
| β-strand | 49-56 | 8 | 9 |
| α-helix | 57-75 | 19 | |
| α-helix | 87-88 | 2 | |
| α-helix | 89-105 | 17 | |
| β-strand | 112-119 | 8 | 9 |
| β-strand | 125-131 | 7 | 9 |
| β-strand | 136-137 | 2 | 9 |
| β-strand | 141-143 | 3 | 10 |
| α-helix | 146-158 | 13 | |
| α-helix | 162-164 | 3 | |
| α-helix | 170-187 | 18 | |
| β-strand | 188 | 1 | 61 |
| β-strand | 194-201 | 8 | 10 |
| β-strand | 205-213 | 9 | 10 |
| α-helix | 220-224 | 5 | |
Chain A: 13 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8 | 1 | 1 |
| β-strand | 12 | 1 | 2 |
| β-strand | 18 | 1 | 2 |
| α-helix | 19-30 | 12 | |
| α-helix | 32-33 | 2 | |
| β-strand | 34-38 | 5 | 3 |
| β-strand | 43-48 | 6 | 3 |
| β-strand | 56 | 1 | 4 |
| α-helix | 58-60 | 3 | |
| β-strand | 65-68 | 4 | 5 |
| β-strand | 71-77 | 7 | 5 |
| α-helix | 79-93 | 15 | |
| α-helix | 94-98 | 5 | |
| α-helix | 99-101 | 3 | |
| α-helix | 104-106 | 3 | |
| α-helix | 107-120 | 14 | |
| β-strand | 125 | 1 | 1 |
| β-strand | 127 | 1 | 6 |
| β-strand | 132-140 | 9 | 5 |
| β-strand | 144-150 | 7 | 5 |
| β-strand | 156-158 | 3 | 5 |
| β-strand | 159 | 1 | 7 |
| β-strand | 161-164 | 4 | 3 |
| α-helix | 168-178 | 11 | |
| α-helix | 185-199 | 15 | |
| β-strand | 209-214 | 6 | 3 |
| α-helix | 219-221 | 3 | |
| β-strand | 224-225 | 2 | 8 |
| β-strand | 235-237 | 3 | 3 |
| α-helix | 238-239 | 2 | |
| α-helix | 240-248 | 9 | |
Chains b and N: 8 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-8 | 6 | 15 |
| β-strand | 11-16 | 6 | 15 |
| β-strand | 20-22 | 3 | 16 |
| β-strand | 25-28 | 4 | 16 |
| β-strand | 34-38 | 5 | 17 |
| β-strand | 41-47 | 7 | 17 |
| α-helix | 49-70 | 22 | |
| α-helix | 73-74 | 2 | |
| α-helix | 75-88 | 14 | |
| β-strand | 95-103 | 9 | 17 |
| β-strand | 107-113 | 7 | 17 |
| β-strand | 120-122 | 3 | 17 |
| β-strand | 124-127 | 4 | 15 |
| α-helix | 129-134 | 6 | |
| α-helix | 135-141 | 7 | |
| α-helix | 148-165 | 18 | |
| β-strand | 166 | 1 | 58 |
| α-helix | 172 | 1 | |
| β-strand | 173-179 | 7 | 15 |
| β-strand | 182-188 | 7 | 15 |
| α-helix | 190-193 | 4 | |
Chain B: 13 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-5 | 4 | |
| β-strand | 12 | 1 | 11 |
| β-strand | 18 | 1 | 11 |
| α-helix | 19-28 | 10 | |
| α-helix | 32-33 | 2 | |
| β-strand | 34-39 | 6 | 12 |
| β-strand | 42-48 | 7 | 12 |
| α-helix | 49 | 1 | |
| β-strand | 56 | 1 | 7 |
| β-strand | 65-69 | 5 | 13 |
| β-strand | 72-78 | 7 | 13 |
| α-helix | 80-101 | 22 | |
| α-helix | 104-106 | 3 | |
| α-helix | 107-123 | 17 | |
| β-strand | 124 | 1 | 14 |
| α-helix | 127-130 | 4 | |
| β-strand | 132-140 | 9 | 13 |
| β-strand | 144-150 | 7 | 13 |
| β-strand | 156-159 | 4 | 13 |
| β-strand | 161-164 | 4 | 12 |
| α-helix | 168-178 | 11 | |
| α-helix | 185-199 | 15 | |
| α-helix | 207-209 | 3 | |
| β-strand | 210-216 | 7 | 12 |
| β-strand | 225-228 | 4 | 12 |
| α-helix | 229-230 | 2 | |
| α-helix | 231-240 | 10 | |
Chains C and Q: 10 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9 | 1 | 18 |
| β-strand | 15 | 1 | 18 |
| α-helix | 16-27 | 12 | |
| α-helix | 29-30 | 2 | |
| β-strand | 31-35 | 5 | 19 |
| β-strand | 40-45 | 6 | 19 |
| β-strand | 53 | 1 | 13 |
| α-helix | 59-60 | 2 | |
| β-strand | 63-66 | 4 | 20 |
| β-strand | 69-75 | 7 | 20 |
| α-helix | 77-98 | 22 | |
| α-helix | 101-103 | 3 | |
| α-helix | 104-117 | 14 | |
| β-strand | 124 | 1 | 14 |
| α-helix | 125-127 | 3 | |
| β-strand | 129-135 | 7 | 20 |
| β-strand | 144-148 | 5 | 20 |
| β-strand | 154-156 | 3 | 20 |
| β-strand | 157 | 1 | 21 |
| β-strand | 159-162 | 4 | 19 |
| α-helix | 166-176 | 11 | |
| β-strand | 178 | 1 | 22 |
| β-strand | 181 | 1 | 22 |
| α-helix | 186-198 | 13 | |
| β-strand | 208-214 | 7 | 19 |
| β-strand | 218-221 | 4 | 19 |
| α-helix | 224-238 | 15 | |
Chains D and R: 14 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6 | 1 | |
| β-strand | 7 | 1 | 23 |
| α-helix | 8 | 1 | |
| β-strand | 13 | 1 | 23 |
| α-helix | 14-24 | 11 | |
| α-helix | 27-28 | 2 | |
| β-strand | 29-34 | 6 | 24 |
| β-strand | 37-43 | 7 | 24 |
| β-strand | 51 | 1 | 21 |
| α-helix | 53-55 | 3 | |
| β-strand | 59-63 | 5 | 25 |
| β-strand | 66-72 | 7 | 25 |
| α-helix | 74-77 | 4 | |
| α-helix | 78-95 | 18 | |
| α-helix | 98-100 | 3 | |
| α-helix | 101-110 | 10 | |
| β-strand | 115 | 1 | 26 |
| β-strand | 126 | 1 | 26 |
| β-strand | 132-140 | 9 | 25 |
| β-strand | 144-150 | 7 | 25 |
| β-strand | 156-158 | 3 | 25 |
| β-strand | 159 | 1 | 27 |
| β-strand | 161-164 | 4 | 24 |
| α-helix | 168-178 | 11 | |
| α-helix | 185-199 | 15 | |
| α-helix | 203-204 | 2 | |
| β-strand | 209-215 | 7 | 24 |
| β-strand | 219-222 | 4 | 24 |
| α-helix | 223-224 | 2 | |
| α-helix | 225-240 | 16 | |
Chains E and S: 8 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 19-29 | 11 | |
| α-helix | 32-33 | 2 | |
| β-strand | 34-38 | 5 | 28 |
| β-strand | 42-48 | 7 | 28 |
| β-strand | 51 | 1 | 29 |
| β-strand | 56 | 1 | 27 |
| β-strand | 58 | 1 | 29 |
| β-strand | 62-66 | 5 | 30 |
| β-strand | 69-75 | 7 | 30 |
| α-helix | 77-98 | 22 | |
| α-helix | 101-103 | 3 | |
| α-helix | 104-117 | 14 | |
| β-strand | 121 | 1 | 31 |
| β-strand | 129-137 | 9 | 30 |
| β-strand | 140-146 | 7 | 30 |
| β-strand | 152-155 | 4 | 30 |
| β-strand | 157-160 | 4 | 28 |
| α-helix | 164-178 | 15 | |
| α-helix | 185-197 | 13 | |
| β-strand | 210-216 | 7 | 28 |
| β-strand | 219-224 | 6 | 28 |
| α-helix | 227-230 | 4 | |
Chains F and T: 11 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-12 | 3 | |
| α-helix | 18-28 | 11 | |
| β-strand | 33-38 | 6 | 32 |
| β-strand | 41-49 | 9 | 32 |
| β-strand | 55 | 1 | 30 |
| α-helix | 56 | 1 | |
| β-strand | 64-66 | 3 | 33 |
| β-strand | 70-76 | 7 | 33 |
| α-helix | 78-99 | 22 | |
| α-helix | 102-104 | 3 | |
| α-helix | 105-118 | 14 | |
| β-strand | 125 | 1 | 31 |
| α-helix | 126-128 | 3 | |
| β-strand | 130-138 | 9 | 33 |
| β-strand | 141-147 | 7 | 33 |
| β-strand | 153-155 | 3 | 33 |
| β-strand | 156 | 1 | 34 |
| β-strand | 158-161 | 4 | 32 |
| α-helix | 165-178 | 14 | |
| α-helix | 185-199 | 15 | |
| α-helix | 200-203 | 4 | |
| β-strand | 208-216 | 9 | 32 |
| β-strand | 225-227 | 3 | 32 |
| α-helix | 229-243 | 15 | |
9 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 |
|---|
| Proteasome subunit alpha type-2 | A, O | protein | 250 | Saccharomyces cerevisiae | P23639 (AlphaFold model) |
| Proteasome subunit alpha type-3 | B, P | protein | 258 | Saccharomyces cerevisiae | P23638 (AlphaFold model) |
| Proteasome subunit alpha type-4 | C, Q | protein | 254 | Saccharomyces cerevisiae | P40303 (AlphaFold model) |
| Proteasome subunit alpha type-5 | D, R | protein | 260 | Saccharomyces cerevisiae | P32379 (AlphaFold model) |
| Proteasome subunit alpha type-6 | E, S | protein | 234 | Saccharomyces cerevisiae | P40302 |
| Probable proteasome subunit alpha type-7 | F, T | protein | 288 | Saccharomyces cerevisiae | P21242 |
| Proteasome subunit alpha type-1 | G, U | protein | 252 | Saccharomyces cerevisiae | P21243 |
| Proteasome subunit beta type-2 | H, V | protein | 232 | Saccharomyces cerevisiae | P25043 |
| Proteasome subunit beta type-3 | I, W | protein | 205 | Saccharomyces cerevisiae | P25451 |
| Proteasome subunit beta type-4 | J, X | protein | 198 | Saccharomyces cerevisiae | P22141 |
| Proteasome subunit beta type-5 | K, Y | protein | 212 | Saccharomyces cerevisiae | P30656 |
| Proteasome subunit beta type-6 | L, Z | protein | 222 | Saccharomyces cerevisiae | P23724 |
2 more molecules are not listed.
Sequence of entity 1 (A, O), FASTA
>4QLQ_1 Proteasome subunit alpha type-2 (chains A, O)
MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSET
LSKVSLLTPDIGAVYSGMGPDYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQE
ATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWKATAIGKGSVAAKTFLEKRWN
DELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTS
QEINDRLEAL
Sequence of entity 2 (B, P), FASTA
>4QLQ_2 Proteasome subunit alpha type-3 (chains B, P)
MGSRRYDSRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQD
TSTEKLYKLNDKIAVAVAGLTADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQ
GYTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGWKAISVGANTSAAQTLLQMDY
KDDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILV
KTGITKKDEDEEADEDMK
Sequence of entity 3 (C, Q), FASTA
>4QLQ_3 Proteasome subunit alpha type-4 (chains C, Q)
MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRIT
PSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRY
TQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYD
RKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEK
QEQQEQDKKKKSNH
Sequence of entity 4 (D, R), FASTA
>4QLQ_4 Proteasome subunit alpha type-5 (chains D, R)
MFLTRSEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLE
SDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLA
LRFGEGASGEERLMSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQ
AELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELI
KELKEKEAAESPEEADVEMS
Sequence of entity 5 (E, S), FASTA
>4QLQ_5 Proteasome subunit alpha type-6 (chains E, S)
MFRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQ
KKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNT
QSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLDTFI
KIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI
Sequence of entity 6 (F, T), FASTA
>4QLQ_6 Probable proteasome subunit alpha type-7 (chains F, T)
MTSIGTGYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLV
PQKNVKIQVVDRHIGCVYSGLIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYV
QAHTLYNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGYKGAATGKGRQSAKAELEKLV
DHHPEGLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAI
DFAQKEINGDDDEDEDDSDNVMSSDDENAPVATNANATTDQEGDIHLE
Sequence of entity 7 (G, U), FASTA
>4QLQ_7 Proteasome subunit alpha type-1 (chains G, U)
MSGAAAASAAGYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVP
DKLLDPTTVSYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKR
MANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITT
NLENHFKKSKIDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAEN
IEERLVAIAEQD
Sequence of entity 8 (H, V), FASTA
>4QLQ_8 Proteasome subunit beta type-2 (chains H, V)
TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIG
SNIELHSLYTSREPRVVSALQMLKQHLFKYQGHIGAYLIVAGVDPTGSHLFSIHAHGSTD
VGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAIQAGIWNDLGSGSNVDVCVMEI
GKDAEYLRNYLTPNVREEKQKSYKFPRGTTAVLKESIVNICDIQEEQVDITA
Sequence of entity 9 (I, W), FASTA
>4QLQ_9 Proteasome subunit beta type-3 (chains I, W)
MSDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFLGITGLATDV
TTLNEMFRYKTNLYKLKEERAIEPETFTQLVSSSLYERRFGPYFVGPVVAGINSKSGKPF
IAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEPEDLFETISQALLNAADRDAL
SGWGAVVYIIKKDEVVKRYLKMRQD
Sequence of entity 10 (J, X), FASTA
>4QLQ_10 Proteasome subunit beta type-4 (chains J, X)
MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYI
QANIQLYSIREDYELSPQAVSSFVRQELAKSIRSRRPYQVNVLIGGYDKKKNKPELYQID
YLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDLLKLCVQELEKRMPMDFKGVI
VKIVDKDGIRQVDDFQAQ
Sequence of entity 11 (K, Y), FASTA
>4QLQ_11 Proteasome subunit beta type-5 (chains K, Y)
TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLG
SQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGT
RLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAAHRDAYSGGSVNLYHV
TEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG
Sequence of entity 12 (L, Z), FASTA
>4QLQ_12 Proteasome subunit beta type-6 (chains L, Z)
QFNPYGDNGGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAAD
GDALVKRFKNSVKWYHFDHNDKKLSINSAARNIQHLLYGKRFFPYYVHTIIAGLDEDGKG
AVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVNFKNQYEPGTNGKVKKPLKYLSVEEV
IKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEFYELKRD
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| 38N | N-(morpholin-4-ylacetyl)-L-alanyl-N-[(2S,4R)-1-cyclohexyl-5-hydroxy-4-methyl-3-… | C31 H48 N4 O7 | 4 |
| MG | Magnesium ion | Mg | 8 |
Water and common crystallization additives (MES) are not listed.
Primary citation
Structure-based design of beta 1i or beta 5i specific inhibitors of human immunoproteasomes. De Bruin, G., Huber, E.M., Xin, B.T. et al. J Med Chem (2014) 57:6197-6209. DOI 10.1021/jm500716s · PubMed
Other PDB entries of the same protein (UniProt P23639 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1RYP 1.9 Å, Crystal structure of the 20S proteasome from yeast at 2.4 Å resolution
- 8RVQ 2.02 Å, 20S proteasome from pre1-1
- 4R17 2.1 Å, Ligand-induced aziridine-formation at subunit beta5 of the yeast 20S proteasome
- 8RVL 2.14 Å, Proteasomal late precursor complex from pre1-1
- 8U7U 2.16 Å, Proteasome 20S Core Particle from Beta 3 D205 deletion
- 1G65 2.25 Å, Crystal structure of epoxomicin:20s proteasome reveals a molecular basis for selectivity…
- 8RVP 2.28 Å, Proteasomal late precursor complex from pre1-1, state 2
- 4QVP 2.3 Å, yCP beta5-M45T mutant in complex with bortezomib
- 5CZ4 2.3 Å, Yeast 20S proteasome at 2.3 A resolution
- 6HWE 2.3 Å, Yeast 20S proteasome beta2-G45A mutant in complex with carfilzomib
- 9GBK 2.39 Å, Blm10-20S proteasome complex from pre1-1
- 1G0U 2.4 Å, A gated channel into the proteasome core particle
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