SAXSdb — 21ip

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Midnolin,Interferon regulatory factor 4

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 205–227	Mutation：A222C	Midnolin × 1 （Q504T8）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；289 K；4% (v/v) tacsimate (pH 4.0) and 12% (w/v) PEG 3,350	Resolution 3.30 Å R-free 0.291

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 21IP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
21IE The MIDN Catch-IRF4 (A8S) fusion protein Deposited 2025-12-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 205–226（22 aa）	Mutation：A222M	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；4%(v/v) tacsimate (pH 4.0) and 12%(w/v) PEG 3,350	Resolution 3.24 Å R-free 0.294
21IK The MIDN Catch-IRF4 (V2T) fusion protein Deposited 2025-12-13	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 205–227（23 aa）	Mutation：V216T	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；4% (v/v) tacsimate (pH 4.0) and 20% (w/v) polyethylene glycol (PEG) 3,350.	Resolution 2.99 Å R-free 0.281
2DLL Solution structure of the IRF domain of human interferon regulator factors 4 Deposited 2006-04-20	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–130（109 aa） Fragment：IRF domain, residues 8-115	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；293 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.23mM 13C, 15N-labeled protein; 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
6TD4 IRF4 DNA-binding domain surface entropy mutant apo structure Deposited 2019-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 20–132（113 aa）	Mutation：E45A E46A K47A C99A	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；25 % PEG 3350, 0.1 M HEPES pH 7.5	Resolution 1.71 Å R-free 0.245
7JM4 IRF Transcription Factor Deposited 2020-07-31	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 21–129（109 aa） Chain B 21–129（109 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；10 % PEG 4000, 0.1 M Na acetate pH 4.6	Resolution 2.95 Å R-free 0.205
7JM4 IRF Transcription Factor Deposited 2020-07-31	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain G 21–129（109 aa） Chain H 21–129（109 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；10 % PEG 4000, 0.1 M Na acetate pH 4.6	Resolution 2.95 Å R-free 0.205
7O56 X-ray Structure of Interferon Regulatory Factor 4 DNA binding domain bound to an interferon-stimulated response element solved by Phosphorus and Sulphur SAD methods Deposited 2021-04-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: pentameric	Chain A 20–139（120 aa） Chain B 20–139（120 aa） Chain C 20–139（120 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.2；293 K；0.1M sodium acetate, 5% PEG 4000, 10mM EDTA	Resolution 2.60 Å R-free 0.241
7OGS X-ray Structure of Interferon Regulatory Factor 4 DNA binding domain bound to an interferon-stimulated response element Deposited 2021-05-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 20–139（120 aa） Chain B 20–139（120 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；0.1M Bis Tris pH 5.5, 0.2M ammonium acetate, 25% PEG 3350	Resolution 2.37 Å R-free 0.249
7OGS X-ray Structure of Interferon Regulatory Factor 4 DNA binding domain bound to an interferon-stimulated response element Deposited 2021-05-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain E 20–139（120 aa） Chain F 20–139（120 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；0.1M Bis Tris pH 5.5, 0.2M ammonium acetate, 25% PEG 3350	Resolution 2.37 Å R-free 0.249
7OOT X-ray Structure of Interferon Regulatory Factor 4 DNA binding domain bound to an interferon-stimulated response element Deposited 2021-05-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 20–139（120 aa） Chain B 20–139（120 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；0.1M Tris HCl pH 8.5, 30% PEG 4000, 0.2M lithium sulfate	Resolution 2.25 Å R-free 0.238
9TOY Investigating the binding mechanism of Interferon Regulatory Factor 4 to DNA in the context of Multiple Myeloma Deposited 2025-12-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 20–139（120 aa） Chain B 20–139（120 aa）	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；0.2M Calcium Acetate, 0.1M MES pH 6, 20% PEG 8000	Resolution 2.10 Å R-free 0.258
9TOY Investigating the binding mechanism of Interferon Regulatory Factor 4 to DNA in the context of Multiple Myeloma Deposited 2025-12-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain D 20–139（120 aa） Chain F 20–139（120 aa）	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；0.2M Calcium Acetate, 0.1M MES pH 6, 20% PEG 8000	Resolution 2.10 Å R-free 0.258
9VE3 The MIDN Catch-IRF4 (V2L) fusion protein Deposited 2025-06-09	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 205–227（23 aa）	Mutation：V216L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；2% (v/v) tacsimate (pH 5.0), 0.1 M sodium citrate, and 16% (w/v) PEG 3,350	Resolution 2.10 Å R-free 0.263
9VE4 The MIDN Catch-IRF4 fusion protein Deposited 2025-06-09	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 205–227（23 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；6% (v/v) tacsimate (pH 4.0) and 12% (w/v) polyethylene glycol (PEG) 3,350	Resolution 2.55 Å R-free 0.281
9VE5 The MIDN Catch-IRF4 (V2Y) fusion protein Deposited 2025-06-09	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 205–227（23 aa）	Mutation：V216Y	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；0.15 M cesium chloride and 15% (w/v) PEG 3,350	Resolution 3.20 Å R-free 0.276
9VE6 The MIDN Catch-IRF4 (F6Y) fusion protein Deposited 2025-06-09	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 205–227（23 aa）	Mutation：F220Y	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；6% (v/v) tacsimate (pH 4.0) and 12% (w/v) polyethylene glycol (PEG) 3,350	Resolution 2.80 Å R-free 0.296
9VE7 The MIDN Catch-IRF4 (A8V) fusion protein Deposited 2025-06-09	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 205–227（23 aa）	Mutation：A222V	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；0.2 M sodium malonate (pH 4.0) and 12% (w/v) PEG 3,350	Resolution 2.15 Å R-free 0.254
9VE8 The MIDN Catch-IRF4 (A8L) fusion protein Deposited 2025-06-09	Different mutation/modification Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 205–227（23 aa）	Mutation：A222L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；4% (v/v) tacsimate (pH 4.0) and 12% (w/v) PEG 3,350	Resolution 2.85 Å R-free 0.274
9VEA The MIDN Catch-IRF4 (A8I) fusion protein Deposited 2025-06-09	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 205–227（23 aa）	Mutation：A222I	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；0.1 M ammonium tartrate (pH 7.0) and 12% (w/v) PEG 3,350	Resolution 3.60 Å R-free 0.272
9VEH The MIDN Catch-IRF4 (A8M) fusion protein Deposited 2025-06-09	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 205–227（23 aa）	Mutation：A222M	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；0.1 M ammonium tartrate (pH 7.0) and 12% (w/v) PEG 3,350	Resolution 2.00 Å R-free 0.287

17 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	IRF4_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 48–68； UniProt 205–227

Midnolin,Interferon regulatory factor 4

Homo sapiens

UniProt Q504T8

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 111–157 Chain B； UniProt 265–334	Mutation：A222C	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；289 K；4% (v/v) tacsimate (pH 4.0) and 12% (w/v) PEG 3,350	Resolution 3.30 Å R-free 0.291

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 21IP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
21IE The MIDN Catch-IRF4 (A8S) fusion protein Deposited 2025-12-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 113–157（45 aa） Chain B 265–334（70 aa）	Mutation：A222M	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；4%(v/v) tacsimate (pH 4.0) and 12%(w/v) PEG 3,350	Resolution 3.24 Å R-free 0.294
21IK The MIDN Catch-IRF4 (V2T) fusion protein Deposited 2025-12-13	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 111–157（47 aa） Chain B 265–334（70 aa）	Mutation：V216T	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；4% (v/v) tacsimate (pH 4.0) and 20% (w/v) polyethylene glycol (PEG) 3,350.	Resolution 2.99 Å R-free 0.281
22MM Structure of human 26S proteasome complexed with midnolin(1-111+337-468) Deposited 2026-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 46 PDB declaration: 46-meric	Chain f 1–18（18 aa） Chain f 107–111（5 aa） Chain f 337–468（132 aa）	Not recorded	ZN ZINC ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 2 LDZ N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-4-methyl-1-oxopentan-2-yl]-L-leucinamide × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.42 Å
9BUI M1A Midnolin-Proteasome (with Ubl) Deposited 2024-05-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 41 PDB declaration: 41-meric	Chain y 1–468（468 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
9BV1 M2A Midnolin-Proteasome (translocating) Deposited 2024-05-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 40 PDB declaration: 40-meric	Chain y 1–468（468 aa）	Not recorded	ZN ZINC ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
9BV2 M2B Midnolin-Proteasome (translocating) Deposited 2024-05-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 40 PDB declaration: 40-meric	Chain y 1–468（468 aa）	Not recorded	ZN ZINC ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9BV3 M1B Midnolin-Proteasome Deposited 2024-05-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 40 PDB declaration: 40-meric	Chain y 2–468（467 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
9M2W The cryo-EM structure of 26S proteasome-Midnolin complex in the MD state Deposited 2025-02-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain u 1–468（468 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.31 Å
9MBO Focused refinement of RPN1 and the C-terminal helix of midnolin in the substrate-engaged human 26S proteasome Deposited 2025-03-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–468（468 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.83 Å
9MBP Substrate-engaged human 26S proteasome bound to midnolin with RPT1 at top of spiral staircase Deposited 2025-03-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain f 1–468（468 aa）	Not recorded	ZN ZINC ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 2 LDZ N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-4-methyl-1-oxopentan-2-yl]-L-leucinamide × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.75 Å
9MBQ Substrate-engaged human 26S proteasome bound to midnolin with RPT5 at top of spiral staircase Deposited 2025-03-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain f 1–468（468 aa）	Not recorded	ZN ZINC ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 LDZ N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-4-methyl-1-oxopentan-2-yl]-L-leucinamide × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.08 Å
9NKG Structure of substrate engaged MIDN-bound human 26S proteasome, EB-MIDN (Composite map) Deposited 2025-02-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain z 1–468（468 aa）	Not recorded	LDZ N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-4-methyl-1-oxopentan-2-yl]-L-leucinamide × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；50 mM Tris, pH 7.5, 150 mM NaCl, 20 mM KCl,5 mM MgCl2, 1 mM TECP, cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
9NKI Structure of substrate engaged MIDN-bound human 26S proteasome, EB MIDN_UBL state (Composite map) Deposited 2025-02-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain z 1–468（468 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；50 mM Tris, pH 7.5, 150 mM NaCl, 20 mM KCl,5 mM MgCl2, 1 mM TECP, cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.94 Å
9UF8 The cryo-EM structure of 26S proteasome-Midnolin complex in the MA state Deposited 2025-04-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 47 PDB declaration: 47-meric	Chain u 1–468（468 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.32 Å
9UG9 The cryo-EM structure of 26S proteasome-Midnolin complex MB state Deposited 2025-04-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain u 1–468（468 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9VE3 The MIDN Catch-IRF4 (V2L) fusion protein Deposited 2025-06-09	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 111–157（47 aa） Chain B 265–334（70 aa）	Mutation：V216L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；2% (v/v) tacsimate (pH 5.0), 0.1 M sodium citrate, and 16% (w/v) PEG 3,350	Resolution 2.10 Å R-free 0.263
9VE4 The MIDN Catch-IRF4 fusion protein Deposited 2025-06-09	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 111–157（47 aa） Chain B 265–334（70 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；6% (v/v) tacsimate (pH 4.0) and 12% (w/v) polyethylene glycol (PEG) 3,350	Resolution 2.55 Å R-free 0.281
9VE5 The MIDN Catch-IRF4 (V2Y) fusion protein Deposited 2025-06-09	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 111–157（47 aa） Chain B 265–334（70 aa）	Mutation：V216Y	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；0.15 M cesium chloride and 15% (w/v) PEG 3,350	Resolution 3.20 Å R-free 0.276
9VE6 The MIDN Catch-IRF4 (F6Y) fusion protein Deposited 2025-06-09	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 111–157（47 aa） Chain B 265–334（70 aa）	Mutation：F220Y	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；6% (v/v) tacsimate (pH 4.0) and 12% (w/v) polyethylene glycol (PEG) 3,350	Resolution 2.80 Å R-free 0.296
9VE7 The MIDN Catch-IRF4 (A8V) fusion protein Deposited 2025-06-09	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 112–157（46 aa） Chain B 265–334（70 aa）	Mutation：A222V	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；0.2 M sodium malonate (pH 4.0) and 12% (w/v) PEG 3,350	Resolution 2.15 Å R-free 0.254
9VE8 The MIDN Catch-IRF4 (A8L) fusion protein Deposited 2025-06-09	Different construct Different mutation/modification Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 112–157（46 aa） Chain B 265–334（70 aa）	Mutation：A222L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；4% (v/v) tacsimate (pH 4.0) and 12% (w/v) PEG 3,350	Resolution 2.85 Å R-free 0.274
9VEA The MIDN Catch-IRF4 (A8I) fusion protein Deposited 2025-06-09	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 113–157（45 aa） Chain B 265–334（70 aa）	Mutation：A222I	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；0.1 M ammonium tartrate (pH 7.0) and 12% (w/v) PEG 3,350	Resolution 3.60 Å R-free 0.272
9VEH The MIDN Catch-IRF4 (A8M) fusion protein Deposited 2025-06-09	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 113–157（45 aa） Chain B 265–334（70 aa）	Mutation：A222M	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；0.1 M ammonium tartrate (pH 7.0) and 12% (w/v) PEG 3,350	Resolution 2.00 Å R-free 0.287
9W39 Structure of human 26S proteasome complexed with midnolin, 19S proteasome with Ubl bound Deposited 2025-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 19 PDB declaration: 19-meric	Chain f 1–468（468 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 1 MG MAGNESIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
9WBG Structure of human 26S proteasome complexed with midnolin, 19S proteasome with Ubl and Catch domain resolved Deposited 2025-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 20 PDB declaration: 20-meric	Chain f 1–468（468 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 1 MG MAGNESIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.23 Å

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MIDN_HUMAN
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–47； UniProt 111–157 Author chain B； PDBConstruct 1–70； UniProt 265–334

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	21ip
Deposition date deposition_date	2025-12-14
最后修订 last_revision	2026-02-04
Structure title title	The MIDN Catch-IRF4 (A8C) fusion protein
Keywords keywords	Midnolin, IRF4, proteasome, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	15.74 Å
Radius of gyration Rg (electron density) rg_electron	14.31 Å
Forward intensity I(0) i0	4072760.00
Molecular weight molecular_weight	13965.0 kDa
Excluded volume excluded_volume	17335 Å³
Envelope volume envelope_volume	20057 Å³
Hydration-shell volume shell_volume	12129 Å³
Envelope diameter envelope_diameter	52.6 Å
Shell Rg shell_rg	19.85 Å
Envelope Rg envelope_rg	14.52 Å
Shape Rg shape_rg	14.33 Å
Total Rg total_rg	15.40 Å
Total atoms total_atoms	978
Residues n_residues	129
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	56.9 Å
Rg (real space) rg_real	15.66 Å
Rg uncertainty (real space) rg_real_error	0.40 Å
I(0) (real space) i0_real	4.0730e+06
I(0) uncertainty (real space) i0_real_error	4.5200e+04
Rg (reciprocal space) rg_reciprocal	15.67 Å
I(0) (reciprocal space) i0_reciprocal	4073000.0000
Solution quality estimate total_estimate	0.8403
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.4 Å
Skewness Skewness skewness	0.180
Kurtosis Kurtosis kurtosis	-0.283
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	548500.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.650; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 1.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Midnolin,Interferon regulatory factor 4
Molecular weight formula_weight	7481.5 kDa
Mutation mutation	A222C
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	978

SRPEQSVMQALESLTETQVSDFLSGRSPLTLALRVGDHMMFVQLQLAWPACENGCQVTGTFYCCAPPE

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Midnolin
Molecular weight formula_weight	7722.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

PGAVIESFVNHAPGVFSGTFSGTLHPNCQDSSGRPRRDIGTILQILNDLLSATRHYQGMPPSLAQLRCHAGSG

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

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8. Citations (1)

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Unit-cell length a length_a	88.397 Å
Unit-cell length b length_b	88.397 Å
Unit-cell length c length_c	72.692 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 65 2 2
Space-group number int_tables_number	179
Crystal system crystal_system	hexagonal

Resolution resolution	3.300 Å
Low-resolution limit resolution_low	44.200 Å
R factor r_factor	0.2524
R_work r_work	0.2483
R_free r_free	0.2909

fit	/app/data/saxs_computation/1i/21ip/21ip.fit
pddf	/app/data/pr_computation/1i/21ip/21ip.pr.out
profile	/app/data/saxs_computation/1i/21ip/21ip.dat

The MIDN Catch-IRF4 (A8C) fusion protein

1. Protein Identity and Related Structures Protein Identity & Related Structures

Midnolin,Interferon regulatory factor 4

State in the Current Structure

Other States of the Same Protein in the Database

Midnolin,Interferon regulatory factor 4

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)