6FVU: 26S proteasome, s2 state

26S proteasome, s2 state. Determined by electron microscopy at 4.5 Å resolution. Released 22 Aug 2018.

Method: Electron microscopy
Resolution: 4.5 Å
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 47
Atoms: 110,592
Mol. weight: 1583.27 kDa
Ligands: ADP, MG, ATP
Released: 22 Aug 2018

Explore 6FVU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6FVU contains 581 α-helices and 522 β-strands across 47 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 1: 6 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	11-17	7	116
β-strand	20-26	7	116
β-strand	29-31	3	76
β-strand	34-37	4	76
β-strand	43-45	3	117
β-strand	50-55	6	117
α-helix	58-79	22
α-helix	81-83	3
α-helix	84-96	13
β-strand	105-111	7	117
β-strand	117-122	6	117
β-strand	129-131	3	117
β-strand	133-137	5	116
α-helix	144-149	6
α-helix	157-174	18
β-strand	175	1	74
β-strand	182-187	6	116
β-strand	192-197	6	116
α-helix	199-204	6

Chain 2: 6 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	31-36	6	85
β-strand	40-46	7	85
β-strand	49-51	3	71
β-strand	54-57	4	71
β-strand	63-65	3	118
β-strand	70-76	7	118
α-helix	78-99	22
α-helix	102-104	3
α-helix	105-118	14
β-strand	125-133	9	118
β-strand	136-142	7	118
β-strand	148-149	2	118
β-strand	153-157	5	85
α-helix	160-170	11
α-helix	177-192	16
β-strand	202-208	7	85
β-strand	213-220	8	85
α-helix	225-228	4
β-strand	241-246	6	119

Chain 3: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	5-8	4
β-strand	11-16	6	119
β-strand	20-25	6	119
β-strand	29	1	120
β-strand	37	1	120
β-strand	43-46	4	121
β-strand	49-55	7	121
α-helix	57-78	22
α-helix	81-83	3
α-helix	84-96	13
β-strand	105-112	8	121
β-strand	119-125	7	121
β-strand	128-131	4	121
β-strand	136-140	5	119
α-helix	143-153	11
α-helix	160-175	16
β-strand	178	1	65
β-strand	186-191	6	119
β-strand	195-200	6	119
α-helix	201	1

Chain 4: 5 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	122
β-strand	12-18	7	122
β-strand	21-23	3	123
β-strand	26-29	4	123
β-strand	35-39	5	124
β-strand	42-48	7	124
α-helix	52-70	19
α-helix	74-76	3
α-helix	77-93	17
β-strand	100-108	9	124
β-strand	113-119	7	124
β-strand	125-127	3	124
β-strand	130-132	3	122
α-helix	138-147	10
α-helix	154-171	18
β-strand	174	1	61
β-strand	179-184	6	122
β-strand	189-192	4	122

Chain 5: 6 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	77-82	6	125
β-strand	87-91	5	125
β-strand	95	1	126
β-strand	100	1	56
β-strand	103	1	126
β-strand	109-113	5	127
β-strand	116-119	4	127
β-strand	121	1	128
α-helix	124-145	22
α-helix	148-150	3
α-helix	151-164	14
β-strand	173	1	128
β-strand	174-180	7	127
β-strand	184-190	7	127
β-strand	196-199	4	127
β-strand	201-205	5	125
α-helix	208-217	10
α-helix	225-242	18
β-strand	243	1	54
β-strand	249-255	7	125
β-strand	260-267	8	125
α-helix	268-279	12

Chain 6: 6 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	19-24	6	3
β-strand	29-34	6	3
β-strand	37-39	3	4
β-strand	42-45	4	4
β-strand	52-53	2	5
β-strand	58-64	7	5
α-helix	66-85	20
α-helix	90-93	4
α-helix	94-107	14
β-strand	115-122	8	5
β-strand	128-133	6	5
β-strand	139-141	3	5
β-strand	144-148	5	3
α-helix	151-158	8
β-strand	168	1	6
β-strand	177	1	6
α-helix	178-182	5
α-helix	185-201	17
β-strand	203	1	44
β-strand	209-215	7	3
β-strand	220-226	7	3

Chain 7: 7 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	40-41	2	11
β-strand	44-48	5	12
β-strand	52-58	7	12
β-strand	60-63	4	11
β-strand	66-70	5	11
β-strand	75-77	3	11
β-strand	82-89	8	11
α-helix	90-107	18
α-helix	122-139	18
β-strand	145-152	8	11
β-strand	158-164	7	11
β-strand	170-171	2	11
β-strand	174-176	3	12
α-helix	178-181	4
α-helix	184-191	8
α-helix	198-200	3
α-helix	203-220	18
β-strand	221	1	36
β-strand	228-234	7	12
β-strand	238-245	8	12
α-helix	255-257	3

Chain a: 9 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	26-31	6
α-helix	32-34	3
β-strand	42-46	5	1
β-strand	51-56	6	1
β-strand	72-74	3	2
β-strand	80-84	5	2
α-helix	87-108	22
α-helix	111-113	3
α-helix	114-127	14
α-helix	135-137	3
β-strand	140-146	7	2
β-strand	152-157	6	2
β-strand	163-166	4	2
β-strand	169-171	3	1
α-helix	175-189	15
α-helix	199-214	16
β-strand	223-229	7	1
β-strand	232-235	4	1
α-helix	238-249	12

39 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-1	A, a	protein	242	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P21243 (AlphaFold model)
Proteasome subunit alpha type-2	B, b	protein	249	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P23639 (AlphaFold model)
Proteasome subunit alpha type-3	C, c	protein	244	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P23638 (AlphaFold model)
Proteasome subunit alpha type-4	D, d	protein	251	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P40303 (AlphaFold model)
Proteasome subunit alpha type-5	E, e	protein	249	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P32379
Proteasome subunit alpha type-6	F, f	protein	231	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P40302
Probable proteasome subunit alpha type-7	G, g	protein	242	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P21242
Proteasome subunit beta type-1	1, h	protein	196	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P38624
Proteasome subunit beta type-2	2, i	protein	226	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P25043
Proteasome subunit beta type-3	3, j	protein	204	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P25451
Proteasome subunit beta type-4	4, k	protein	195	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P22141
Proteasome subunit beta type-5	5, l	protein	212	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P30656

21 more molecules are not listed.

Sequence of entity 1 (A, a), FASTA

>6FVU_1 Proteasome subunit alpha type-1 (chains A, a)
AGYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTV
SYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYT
QRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITTNLENHFKKS
KIDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAENIEERLVAIA
EQ

Sequence of entity 2 (B, b), FASTA

>6FVU_2 Proteasome subunit alpha type-2 (chains B, b)
TDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSETL
SKVSLLTPDIGAVYSGMGPDYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQEA
TQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWKATAIGKGSVAAKTFLEKRWND
ELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTSQ
EINDRLEAL

Sequence of entity 3 (C, c), FASTA

>6FVU_3 Proteasome subunit alpha type-3 (chains C, c)
GSRRYDSRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQDT
STEKLYKLNDKIAVAVAGLTADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQG
YTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGWKAISVGANTSAAQTLLQMDYK
DDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILVK
TGIT

Sequence of entity 4 (D, d), FASTA

>6FVU_4 Proteasome subunit alpha type-4 (chains D, d)
YDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSK
VSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQS
GGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYDRKE
PPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEKQEQ
QEQDKKKKSNH

Sequence of entity 5 (E, e), FASTA

>6FVU_5 Proteasome subunit alpha type-5 (chains E, e)
FLTRSEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLES
DSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLAL
RFGEGASGEERLMSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQA
ELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELIK
ELKEKEAAE

Sequence of entity 6 (F, f), FASTA

>6FVU_6 Proteasome subunit alpha type-6 (chains F, f)
NNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKI
IKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSY
GGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLDTFIKID
GNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI

Sequence of entity 7 (G, g), FASTA

>6FVU_7 Probable proteasome subunit alpha type-7 (chains G, g)
GYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLVPQKNVK
IQVVDRHIGCVYSGLIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYVQAHTLY
NSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGYKGAATGKGRQSAKAELEKLVDHHPEG
LSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAIDFAQKE
IN

Sequence of entity 8 (1, h), FASTA

>6FVU_8 Proteasome subunit beta type-1 (chains 1, h)
TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQ
YHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVH
KLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSLSQAIKWDGSSGGVIRMVVLTA
AGVERLIFYPDEYEQL

Sequence of entity 9 (2, i), FASTA

>6FVU_9 Proteasome subunit beta type-2 (chains 2, i)
TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIG
SNIELHSLYTSREPRVVSALQMLKQHLFKYQGHIGAYLIVAGVDPTGSHLFSIHAHGSTD
VGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAIQAGIWNDLGSGSNVDVCVMEI
GKDAEYLRNYLTPNVREEKQKSYKFPRGTTAVLKESIVNICDIQEE

Sequence of entity 10 (3, j), FASTA

>6FVU_10 Proteasome subunit beta type-3 (chains 3, j)
SDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFLGITGLATDVT
TLNEMFRYKTNLYKLKEERAIEPETFTQLVSSSLYERRFGPYFVGPVVAGINSKSGKPFI
AGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEPEDLFETISQALLNAADRDALS
GWGAVVYIIKKDEVVKRYLKMRQD

Sequence of entity 11 (4, k), FASTA

>6FVU_11 Proteasome subunit beta type-4 (chains 4, k)
MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYI
QANIQLYSIREDYELSPQAVSSFVRQELAKSIRSRRPYQVNVLIGGYDKKKNKPELYQID
YLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDLLKLCVQELEKRMPMDFKGVI
VKIVDKDGIRQVDDF

Sequence of entity 12 (5, l), FASTA

>6FVU_12 Proteasome subunit beta type-5 (chains 5, l)
TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLG
SQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGT
RLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAAHRDAYSGGSVNLYHV
TEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	1
MG	Magnesium ion	Mg	6
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	5

Primary citation

Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating. Eisele, M.R., Reed, R.G., Rudack, T. et al. Cell Rep (2018) 24:1301-1315.e5. DOI 10.1016/j.celrep.2018.07.004 · PubMed

Other PDB entries of the same protein (UniProt P21243 (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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