35ZR: 26S proteasome regulatory subunit 7 homolog

yeast 26S proteasome base assembly intermediate, Hsm3-Rpt1-Rpt2 (base-Hsm3-Nas6 with Rpt4-EQ). Determined by electron microscopy at 2.99 Å resolution. Released 19 Aug 2026.

Method: Electron microscopy
Resolution: 2.99 Å
Organism: Saccharomyces cerevisiae
Chains: 3
Atoms: 7,786
Mol. weight: 157.57 kDa
Ligands: ATP
Released: 19 Aug 2026

Explore 35ZR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

35ZR contains 73 α-helices and 18 β-strands across 3 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: 18 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	198-201	4	1
α-helix	208-210	3
α-helix	215-225	11
α-helix	227-230	4
α-helix	232-238	7
α-helix	240-243	4
β-strand	245-249	5	1
α-helix	256-266	11
β-strand	270-275	6	1
α-helix	276-279	4
α-helix	288-300	13
β-strand	304-309	6	1
α-helix	312-315	4
β-strand	316	1	2
α-helix	317-318	2
α-helix	328-342	15
β-strand	349-355	7	1
α-helix	358-360	3
β-strand	361	1	2
β-strand	373-376	4	1
α-helix	378-380	3
α-helix	382-393	12
β-strand	398	1	3
α-helix	404-409	6
α-helix	416-432	17
β-strand	438	1	3
α-helix	440-447	8
α-helix	448-452	5

Chain B: 17 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	167-170	4
β-strand	172-174	3	4
α-helix	181-183	3
α-helix	188-194	7
α-helix	195-199	5
α-helix	200-203	4
α-helix	205-211	7
α-helix	214-216	3
β-strand	218-223	6	4
α-helix	229-240	12
α-helix	242	1
β-strand	243-248	6	4
α-helix	249-254	6
α-helix	260-273	14
β-strand	277-282	6	4
α-helix	285-291	7
α-helix	301-315	15
β-strand	322-328	7	4
α-helix	331-333	3
β-strand	347-350	4	4
α-helix	355-366	12
β-strand	371	1	5
α-helix	389-405	17
β-strand	411	1	5
α-helix	413-427	15

Chain D: 38 helices, 0 β-strands

Element	Residues	Length
α-helix	8-20	13
α-helix	29-42	14
α-helix	52-64	13
α-helix	73-83	11
α-helix	89-95	7
α-helix	98-106	9
α-helix	110-121	12
α-helix	128-131	4
α-helix	134-142	9
α-helix	150-163	14
α-helix	167-171	5
α-helix	172-176	5
α-helix	178-187	10
α-helix	190-206	17
α-helix	214-217	4
α-helix	221-227	7
α-helix	231-251	21
α-helix	254-256	3
α-helix	257-260	4
α-helix	264-272	9
α-helix	278-283	6
α-helix	285-295	11
α-helix	304-309	6
α-helix	310-314	5
α-helix	323-329	7
α-helix	332-338	7
α-helix	340-346	7
α-helix	351-353	3
α-helix	354-360	7
α-helix	364-370	7
α-helix	376-380	5
α-helix	384-394	11
α-helix	398-407	10
α-helix	409-416	8
α-helix	427-441	15
α-helix	445-448	4
α-helix	449-451	3
α-helix	452-464	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
26S proteasome regulatory subunit 7 homolog	A	protein	467	Saccharomyces cerevisiae	P33299 (AlphaFold model)
26S proteasome regulatory subunit 4 homolog	B	protein	437	Saccharomyces cerevisiae	P40327 (AlphaFold model)
DNA mismatch repair protein HSM3	D	protein	480	Saccharomyces cerevisiae	P38348 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>35ZR_1 26S proteasome regulatory subunit 7 homolog (chains A)
MPPKEDWEKYKAPLEDDDKKPDDDKIVPLTEGDIQVLKSYGAAPYAAKLKQTENDLKDIE
ARIKEKAGVKESDTGLAPSHLWDIMGDRQRLGEEHPLQVARCTKIIKGNGESDETTTDNN
NSGNSNSNSNQQSTDADEDDEDAKYVINLKQIAKFVVGLGERVSPTDIEEGMRVGVDRSK
YNIELPLPPRIDPSVTMMTVEEKPDVTYSDVGGCKDQIEKLREVVELPLLSPERFATLGI
DPPKGILLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMART
KKACIIFFDEIDAVGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVMFATNRPNT
LDPALLRPGRIDRKVEFSLPDLEGRANIFRIHSKSMSVERGIRWELISRLCPNSTGAELR
SVCTEAGMFAIRARRKVATEKDFLKAVDKVISGYKKFSSTSRYMQYN

Sequence of entity 2 (B), FASTA

>35ZR_2 26S proteasome regulatory subunit 4 homolog (chains B)
MGQGVSSGQDKKKKKGSNQKPKYEPPVQSKFGRKKRKGGPATAEKLPNIYPSTRCKLKLL
RMERIKDHLLLEEEFVSNSEILKPFEKKQEEEKKQLEEIRGNPLSIGTLEEIIDDDHAIV
TSPTMPDYYVSILSFVDKELLEPGCSVLLHHKTMSIVGVLQDDADPMVSVMKMDKSPTES
YSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQT
SATFLRIVGSELIQKYLGDGPRLCRQIFKVAGENAPSIVFIDEIDAIGTKRYDSNSGGER
EIQRTMLELLNQLDGFDDRGDVKVIMATNKIETLDPALIRPGRIDRKILFENPDLSTKKK
ILGIHTSKMNLSEDVNLETLVTTKDDLSGADIQAMCTEAGLLALRERRMQVTAEDFKQAK
ERVMKNKVEENLEGLYL

Sequence of entity 3 (D), FASTA

>35ZR_3 DNA mismatch repair protein HSM3 (chains D)
MSEKETNYVENLLTQLENELNEDNLPEDINTLLRKCSLNLVTVVSLPDMDVKPLLATIKR
FLTSNVSYDSLNYDYLLDVVDKLVPMADFDDVLEVYSAEDLVKALRSEIDPLKVAACRVI
ENSQPKGLFATSNIIDILLDILFDEKVENDKLITAIEKALERLSTDELIRRRLFDNNLPY
LVSVKGRMETVSFVRLIDFLTIEFQFISGPEFKDIIFCFTKEEILKSVEDILVFIELVNY
YTKFLLEIRNQDKYWALRHVKKILPVFAQLFEDTENYPDVRAFSTNCLLQLFAEVSRIEE
DEYSLFKTMDKDSLKIGSEAKLITEWLELINPQYLVKYHKDVVENYFHVSGYSIGMLRNL
SADEECFNAIRNKFSAEIVLRLPYLEQMQVVETLTRYEYTSKFLLNEMPKVMGSLIGDGS
AGAIIDLETVHYRNSALRNLLDKGEEKLSVWYEPLLREYSKAVNGKNYSTGSETKIADCR

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2

Primary citation

Chaperones shape the conformational landscape of 26S-proteasome-base assembly for allosteric ATPase motor activation. Hsieh, H.H., Martin, A. bioRxiv (2026). DOI 10.64898/2026.06.01.729410 · PubMed

Other PDB entries of the same protein (UniProt P33299 (AlphaFold model), which also has an AlphaFold model), best resolution first:

35ZW 3.31 Å, yeast 26S proteasome base assembly intermediate, Hsm3-Rpt1-Rpt2-Rpt3-Rpt4-Rpt5…
9CGC 3.61 Å, Yeast 26S proteasome non-substrate-engaged (S1 state)
3VLF 3.8 Å, Crystal structure of yeast proteasome interacting protein
4A3V 3.8 Å, yeast regulatory particle proteasome assembly chaperone Hsm3 in complex with Rpt1…
6J2Q 3.8 Å, Yeast proteasome in Ub-accepted state (C1-b)
6J2X 3.8 Å, Yeast proteasome in resting state (C1-a)
36BM 3.82 Å, yeast 26S proteasome base assembly intermediate, base-Hsm3-Nas6 with Rpt4-EQ
36BL 3.91 Å, yeast 26S proteasome base assembly intermediate, base-Rpn14-Hsm3-Nas6(2) with Rpt4-EQ
36BD 3.93 Å, yeast 26S proteasome base assembly intermediate, base-Rpn14-Hsm3-Nas6 with Rpt4-EQ
5MP9 4.1 Å, 26S proteasome in presence of ATP (s1)
6FVT 4.1 Å, 26S proteasome, s1 state
6EF3 4.17 Å, Yeast 26S proteasome bound to ubiquitinated substrate (4D motor state)

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