22MM image
Deposition Date 2026-01-16
Release Date 2026-04-01
Last Version Date 2026-04-08
Entry Detail
PDB ID:
22MM
Keywords:
Title:
Structure of human 26S proteasome complexed with midnolin(1-111+337-468)
Biological Source:
Source Organism(s):
Expression System(s):
Method Details:
Experimental Method:
Resolution:
3.42 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
Macromolecular Entities
Polymer Type:polypeptide(L)
Molecule:26S proteasome regulatory sub
Chain IDs:K (auth: A)
Chain Length:376
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome regulatory sub
Chain IDs:L (auth: B)
Chain Length:440
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome regulatory sub
Chain IDs:M (auth: C)
Chain Length:398
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome regulatory sub
Chain IDs:N (auth: D)
Chain Length:349
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome 26S subunit, ATPas
Chain IDs:O (auth: E)
Chain Length:403
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome regulatory sub
Chain IDs:P (auth: F)
Chain Length:445
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit alpha type
Chain IDs:Q (auth: G), EA (auth: g)
Chain Length:245
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit alpha type
Chain IDs:R (auth: H), FA (auth: h)
Chain Length:233
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit alpha type
Chain IDs:S (auth: I), GA (auth: i)
Chain Length:260
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit alpha type
Chain IDs:T (auth: J)
Chain Length:248
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit alpha type
Chain IDs:U (auth: K), IA (auth: k)
Chain Length:241
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Isoform Long of Proteasome su
Chain IDs:V (auth: L), JA (auth: l)
Chain Length:268
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit alpha type
Chain IDs:W (auth: M), KA (auth: m)
Chain Length:254
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit beta type-
Chain IDs:X (auth: N), LA (auth: n)
Chain Length:238
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit beta type-
Chain IDs:Y (auth: O), MA (auth: o)
Chain Length:276
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit beta type-
Chain IDs:Z (auth: P), NA (auth: p)
Chain Length:204
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit beta type-
Chain IDs:AA (auth: Q), OA (auth: q)
Chain Length:201
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit beta type-
Chain IDs:BA (auth: R), PA (auth: r)
Chain Length:262
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit beta type-
Chain IDs:CA (auth: S), QA (auth: s)
Chain Length:240
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit beta type-
Chain IDs:DA (auth: T), RA (auth: t)
Chain Length:263
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome non-ATPase reg
Chain IDs:A (auth: U)
Chain Length:953
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome non-ATPase reg
Chain IDs:B (auth: V)
Chain Length:533
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome non-ATPase reg
Chain IDs:C (auth: W)
Chain Length:456
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome non-ATPase reg
Chain IDs:D (auth: X)
Chain Length:422
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome non-ATPase reg
Chain IDs:E (auth: Y)
Chain Length:389
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome non-ATPase reg
Chain IDs:F (auth: Z)
Chain Length:324
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome non-ATPase reg
Chain IDs:G (auth: a)
Chain Length:376
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome non-ATPase reg
Chain IDs:H (auth: c)
Chain Length:398
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome non-ATPase reg
Chain IDs:I (auth: d)
Chain Length:349
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome complex subuni
Chain IDs:J (auth: e)
Chain Length:403
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Midnolin,MCHERRY,fusion tag
Chain IDs:SA (auth: f)
Chain Length:445
Number of Molecules:1
Biological Source:Homo sapiens, Escherichia coli str. K-12 substr. MG1655, synthetic construct
Polymer Type:polypeptide(L)
Molecule:Proteasome subunit alpha type
Chain IDs:HA (auth: j)
Chain Length:248
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:26S proteasome non-ATPase reg
Chain IDs:TA (auth: u)
Chain Length:953
Number of Molecules:1
Biological Source:Homo sapiens
Peptide-like Molecules
PRD_000907
Primary Citation
Structural dynamics of the midnolin-proteasome during ubiquitin-independent substrate turnover.
Nat Commun 17 ? ? (2026)
PMID: 41896529 DOI: 10.1038/s41467-026-71002-0
Primary Citation of related structures
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