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3jc1

Electron cryo-microscopy of the IST1-CHMP1B ESCRT-III copolymer

Method: ELECTRON MICROSCOPY Dmax: 249.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Increased Sodium Tolerance 1 (IST1)

Homo sapiens

UniProt P53990

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 68 PDB declaration: 68-meric（68） Consistent with protein copy count Chain Aa； UniProt 6–187 Chain Ac； UniProt 6–187 Chain Ae； UniProt 6–187 Chain Ag； UniProt 6–187 Chain Ai； UniProt 6–187 Chain Ak； UniProt 6–187 Chain Am； UniProt 6–187 Chain Ao； UniProt 6–187 Chain Aq； UniProt 6–187 Chain As； UniProt 6–187 Chain Au； UniProt 6–187 Chain Aw； UniProt 6–187 Chain Ay； UniProt 6–187 Chain Ba； UniProt 6–187 Chain Bc； UniProt 6–187 Chain Be； UniProt 6–187 Chain Bg； UniProt 6–187 Chain Bi； UniProt 6–187 Chain Bk； UniProt 6–187 Chain Bm； UniProt 6–187 Chain Bo； UniProt 6–187 Chain Bq； UniProt 6–187 Chain Bs； UniProt 6–187 Chain Bu； UniProt 6–187 Chain Bw； UniProt 6–187 Chain By； UniProt 6–187 Chain Ca； UniProt 6–187 Chain Cc； UniProt 6–187 Chain Ce； UniProt 6–187 Chain Cg； UniProt 6–187 Chain Ci； UniProt 6–187 Chain Ck； UniProt 6–187 Chain Cm； UniProt 6–187 Chain Co； UniProt 6–187 Fragment：N-terminal domain (UNP residues 6-187) Charged multivesicular body protein 1b × 34 （Q7LBR1） ELECTRON MICROSCOPY cryo-EM buffer：25 mM Tris, pH 8.0, 25 mM sodium chloride；pH 8；25 mM Tris, pH 8.0, 25 mM sodium chloride cryo-EM vitrification conditions：Deposited 3.5 uL sample, blotted 3-6 seconds (0 mm offset)；Cryogen ETHANE；Deposited 3.5 uL sample, blotted 3-6 seconds (0 mm offset), and plunged into liquid ethane (VITROBOT MARK III). Resolution 4.00 Å

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 3JC1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3FRR Structure of human IST1(NTD) - (residues 1-189)(P21) Deposited 2009-01-08 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 1–189（189 aa） Fragment：UNP residues 1-189
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；296 K；35% pentaethritol propexylate 180mM KCl 50 mM HEPES, pH 7.6 7% ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 296K
Resolution 1.80 Å R-free 0.247
3FRS Structure of human IST1(NTD) (residues 1-189)(p43212) Deposited 2009-01-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 5–189（185 aa） Fragment：UNP residues 1-189
Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；296 K；10mM Tris-HCL, pH 8.0, 350mM NaCl, 1mM DTT, VAPOR DIFFUSION, SITTING DROP, temperature 296K
Resolution 2.61 Å R-free 0.298
4U7E The crystal structure of the complex of LIP5 NTD and IST1 MIM Deposited 2014-07-30 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 341–364（24 aa） Fragment：UNP residues 341-364
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277.15 K；30% (w/v) PEG5000MME, 0.1 M ammonium sulfate , 0.1 M MES
Resolution 1.60 Å R-free 0.201
4U7I Structure of the complex of Spartin MIT and IST1 MIM Deposited 2014-07-30 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 B 341–364（24 aa） Fragment：UNP residues 341-364
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.3；277 K；2.9 M Na-malonate
Resolution 1.79 Å R-free 0.220
4U7Y Structure of the complex of VPS4B MIT and IST1 MIM Deposited 2014-07-31 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 B 341–364（24 aa） Fragment：UNP residues 341-364
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.3；299 K；2.58 M Na-malonate
Resolution 2.50 Å R-free 0.271
4WZX ULK3 regulates cytokinetic abscission by phosphorylating ESCRT-III proteins Deposited 2014-11-20 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 × 2 PDB declaration: dimeric
Chain E 342–364（23 aa） Fragment：MIT-interacting motif (UNP residues 342-364)
Not recorded CO COBALT (II) ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；295 K；50mM MES pH 6.5, 5mM Cobalt chloride, 800mM ammonium sulfate
Resolution 1.39 Å R-free 0.180
6E8G CryoEM reconstruction of IST1-CHMP1B copolymer filament bound to ssDNA at 2.9 Angstrom resolution Deposited 2018-07-29 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 72 PDB declaration: 72-meric
Chain A 1–366（366 aa）
Chain BA 1–366（366 aa）
Chain BB 1–366（366 aa）
Chain C 1–366（366 aa）
Chain DA 1–366（366 aa）
Chain DB 1–366（366 aa）
Chain E 1–366（366 aa）
Chain FA 1–366（366 aa）
Chain FB 1–366（366 aa）
Chain G 1–366（366 aa）
Chain HA 1–366（366 aa）
Chain HB 1–366（366 aa）
Chain I 1–366（366 aa）
Chain JA 1–366（366 aa）
Chain JB 1–366（366 aa）
Chain K 1–366（366 aa）
Chain LA 1–366（366 aa）
Chain LB 1–366（366 aa）
Chain M 1–366（366 aa）
Chain NA 1–366（366 aa）
Chain NB 1–366（366 aa）
Chain O 1–366（366 aa）
Chain PA 1–366（366 aa）
Chain PB 1–366（366 aa）
Chain Q 1–366（366 aa）
Chain RA 1–366（366 aa）
Chain RB 1–366（366 aa）
Chain S 1–366（366 aa）
Chain TA 1–366（366 aa）
Chain TB 1–366（366 aa）
Chain V 1–366（366 aa）
Chain VA 1–366（366 aa）
Chain X 1–366（366 aa）
Chain XA 1–366（366 aa）
Chain Z 1–366（366 aa）
Chain ZA 1–366（366 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；0 mm offset with 10 sec wait time and 2-4 sec blot
Resolution 2.90 Å
6TZ4 CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (right-handed) Deposited 2019-08-10 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 72 PDB declaration: 72-meric
Chain 01 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain AA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain AB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain B 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain CA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain CB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain D 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain EA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain EB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain F 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain GA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain GB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain H 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain IA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain IB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain J 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain KA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain KB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain L 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain MA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain MB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain N 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain OA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain OB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain P 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain QA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain QB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain R 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain SA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain SB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain T 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain UA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain W 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain WA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain Y 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain YA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted with Whatman No. 1 filter paper for 4-8 seconds with a 0 mm offset at 19C and 100 percent humidity before plunging into liquid ethane
Resolution 3.20 Å
6TZ5 CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (left-handed) Deposited 2019-08-10 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 68 PDB declaration: 68-meric
Chain A 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain BA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain BB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain C 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain DA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain DB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain E 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain FA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain FB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain G 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain HA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain HB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain I 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain JA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain JB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain K 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain LA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain LB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain M 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain NA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain NB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain O 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain PA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain PB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain Q 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain RA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain S 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain TA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain V 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain VA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain X 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain XA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain Z 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain ZA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted with Whatman No. 1 filter paper for 4-8 seconds with a 0 mm offset at 19C and 100 percent humidity before plunging into liquid ethane
Resolution 3.10 Å
6TZA CryoEM reconstruction of ESCRT-III filament composed of IST1 NTD R16E K27E double mutant Deposited 2019-08-11 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric
Chain A 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain B 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain C 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain D 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain E 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain F 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain G 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain H 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain I 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain J 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain K 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain L 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain M 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain N 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted with Whatman No. 1 filter paper for 4-8 seconds with a 0 mm offset at 19C and 100 percent humidity before plunging into liquid ethane.
Resolution 7.20 Å
7S7J Structure of Human SPASTIN-IST1 complex. Deposited 2021-09-16 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 × 2 PDB declaration: dimeric
Chain B 342–364（23 aa） Fragment：UNP residues 342-364
Not recorded PG4 TETRAETHYLENE GLYCOL × 1 CA CALCIUM ION × 1 PGE TRIETHYLENE GLYCOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；278 K；40% v/v PEG 300, 100 mM Sodium cacodylate / Hydrochloric acid pH=6.5, 200 mM Calcium Acetate
Resolution 1.15 Å R-free 0.157
8UC6 Calpain-7:IST1 Complex Deposited 2023-09-25 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 G 335–379（45 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.2；294 K；Both proteins were purified and concentrated to 20 mg/ml in buffer containing 25 mM Tris, pH 7.2, 150 mM NaCl, 1 mM TCEP, 0.5 mM EDTA. The proteins were mixed in a 1:2 molar ratio (CAPN7:IST1). Crystals grew at 21 C (294 K) in Rigaku Wizard Cryo condition D5 (25% (v/v) 1,2-Porpanediol, 100 mM Sodium phosphate dibasic/Citric acid pH 4.2, 5% (w/v) PEG 3000, 10% (v/v) Glycerol. Crystals were transferred briefly to crystallization buffer supplemented with 25% added glycerol prior to plunging in liquid nitrogen
Resolution 2.70 Å R-free 0.285
8UC6 Calpain-7:IST1 Complex Deposited 2023-09-25 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 335–379（45 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.2；294 K；Both proteins were purified and concentrated to 20 mg/ml in buffer containing 25 mM Tris, pH 7.2, 150 mM NaCl, 1 mM TCEP, 0.5 mM EDTA. The proteins were mixed in a 1:2 molar ratio (CAPN7:IST1). Crystals grew at 21 C (294 K) in Rigaku Wizard Cryo condition D5 (25% (v/v) 1,2-Porpanediol, 100 mM Sodium phosphate dibasic/Citric acid pH 4.2, 5% (w/v) PEG 3000, 10% (v/v) Glycerol. Crystals were transferred briefly to crystallization buffer supplemented with 25% added glycerol prior to plunging in liquid nitrogen
Resolution 2.70 Å R-free 0.285
8V2Q CHMP1B/IST1 ssRNA bound copolymer Deposited 2023-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 182 PDB declaration: 182-meric
Chain B 1–364（364 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.95 Å
8V2R CryoEM of ssDNA bound CHMP1B/IST1 copolymer assembly Deposited 2023-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric
Chain B 1–364（364 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.01 Å
8V2S CHMP1B/IST1 dsDNA bound copolymer Deposited 2023-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric
Chain B 1–364（364 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.72 Å

15 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IST1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain Aa； PDBConstruct 1–182； UniProt 6–187 Author chain Ac； PDBConstruct 1–182； UniProt 6–187 Author chain Ae； PDBConstruct 1–182； UniProt 6–187 Author chain Ag； PDBConstruct 1–182； UniProt 6–187 Author chain Ai； PDBConstruct 1–182； UniProt 6–187 Author chain Ak； PDBConstruct 1–182； UniProt 6–187 Author chain Am； PDBConstruct 1–182； UniProt 6–187 Author chain Ao； PDBConstruct 1–182； UniProt 6–187 Author chain Aq； PDBConstruct 1–182； UniProt 6–187 Author chain As； PDBConstruct 1–182； UniProt 6–187 Author chain Au； PDBConstruct 1–182； UniProt 6–187 Author chain Aw； PDBConstruct 1–182； UniProt 6–187 Author chain Ay； PDBConstruct 1–182； UniProt 6–187 Author chain Ba； PDBConstruct 1–182； UniProt 6–187 Author chain Bc； PDBConstruct 1–182； UniProt 6–187 Author chain Be； PDBConstruct 1–182； UniProt 6–187 Author chain Bg； PDBConstruct 1–182； UniProt 6–187 Author chain Bi； PDBConstruct 1–182； UniProt 6–187 Author chain Bk； PDBConstruct 1–182； UniProt 6–187 Author chain Bm； PDBConstruct 1–182； UniProt 6–187 Author chain Bo； PDBConstruct 1–182； UniProt 6–187 Author chain Bq； PDBConstruct 1–182； UniProt 6–187 Author chain Bs； PDBConstruct 1–182； UniProt 6–187 Author chain Bu； PDBConstruct 1–182； UniProt 6–187 Author chain Bw； PDBConstruct 1–182； UniProt 6–187 Author chain By； PDBConstruct 1–182； UniProt 6–187 Author chain Ca； PDBConstruct 1–182； UniProt 6–187 Author chain Cc； PDBConstruct 1–182； UniProt 6–187 Author chain Ce； PDBConstruct 1–182； UniProt 6–187 Author chain Cg； PDBConstruct 1–182； UniProt 6–187 Author chain Ci； PDBConstruct 1–182； UniProt 6–187 Author chain Ck； PDBConstruct 1–182； UniProt 6–187 Author chain Cm； PDBConstruct 1–182； UniProt 6–187 Author chain Co； PDBConstruct 1–182； UniProt 6–187

Charged multivesicular body protein 1b

Homo sapiens

UniProt Q7LBR1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 68 PDB declaration: 68-meric（68） Consistent with protein copy count Chain Ab； UniProt 4–163 Chain Ad； UniProt 4–163 Chain Af； UniProt 4–163 Chain Ah； UniProt 4–163 Chain Aj； UniProt 4–163 Chain Al； UniProt 4–163 Chain An； UniProt 4–163 Chain Ap； UniProt 4–163 Chain Ar； UniProt 4–163 Chain At； UniProt 4–163 Chain Av； UniProt 4–163 Chain Ax； UniProt 4–163 Chain Az； UniProt 4–163 Chain Bb； UniProt 4–163 Chain Bd； UniProt 4–163 Chain Bf； UniProt 4–163 Chain Bh； UniProt 4–163 Chain Bj； UniProt 4–163 Chain Bl； UniProt 4–163 Chain Bn； UniProt 4–163 Chain Bp； UniProt 4–163 Chain Br； UniProt 4–163 Chain Bt； UniProt 4–163 Chain Bv； UniProt 4–163 Chain Bx； UniProt 4–163 Chain Bz； UniProt 4–163 Chain Cb； UniProt 4–163 Chain Cd； UniProt 4–163 Chain Cf； UniProt 4–163 Chain Ch； UniProt 4–163 Chain Cj； UniProt 4–163 Chain Cl； UniProt 4–163 Chain Cn； UniProt 4–163 Chain Cp； UniProt 4–163 Fragment：UNP residues 4-163 Increased Sodium Tolerance 1 (IST1) × 34 （P53990） ELECTRON MICROSCOPY cryo-EM buffer：25 mM Tris, pH 8.0, 25 mM sodium chloride；pH 8；25 mM Tris, pH 8.0, 25 mM sodium chloride cryo-EM vitrification conditions：Deposited 3.5 uL sample, blotted 3-6 seconds (0 mm offset)；Cryogen ETHANE；Deposited 3.5 uL sample, blotted 3-6 seconds (0 mm offset), and plunged into liquid ethane (VITROBOT MARK III). Resolution 4.00 Å

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 3JC1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4TXQ Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM Deposited 2014-07-04 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 C 176–199（24 aa） Fragment：UNP residues 176-199
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277.15 K；Protein mixture was added in 1:1 ratio with a solution of 16% MPD, 0.1 M Tris and equilibrated against a mother liquid of 8% MPD, 0.1 M Tris
Resolution 2.21 Å R-free 0.227
4TXQ Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM Deposited 2014-07-04 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 176–199（24 aa） Fragment：UNP residues 176-199
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277.15 K；Protein mixture was added in 1:1 ratio with a solution of 16% MPD, 0.1 M Tris and equilibrated against a mother liquid of 8% MPD, 0.1 M Tris
Resolution 2.21 Å R-free 0.227
4TXR Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM and CHMP5 MIM Deposited 2014-07-04 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 × 3 PDB declaration: trimeric
Chain B 176–199（24 aa） Fragment：UNP residues 176-199
Not recorded ACT ACETATE ION × 1 EDO 1,2-ETHANEDIOL × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277.15 K；19% PEG 4000, 0.025 M sodium acetate
Resolution 1.00 Å R-free 0.180
6E8G CryoEM reconstruction of IST1-CHMP1B copolymer filament bound to ssDNA at 2.9 Angstrom resolution Deposited 2018-07-29 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 72 PDB declaration: 72-meric
Chain AA 1–199（199 aa）
Chain AB 1–199（199 aa）
Chain B 1–199（199 aa）
Chain CA 1–199（199 aa）
Chain CB 1–199（199 aa）
Chain D 1–199（199 aa）
Chain EA 1–199（199 aa）
Chain EB 1–199（199 aa）
Chain F 1–199（199 aa）
Chain GA 1–199（199 aa）
Chain GB 1–199（199 aa）
Chain H 1–199（199 aa）
Chain IA 1–199（199 aa）
Chain IB 1–199（199 aa）
Chain J 1–199（199 aa）
Chain KA 1–199（199 aa）
Chain KB 1–199（199 aa）
Chain L 1–199（199 aa）
Chain MA 1–199（199 aa）
Chain MB 1–199（199 aa）
Chain N 1–199（199 aa）
Chain OA 1–199（199 aa）
Chain OB 1–199（199 aa）
Chain P 1–199（199 aa）
Chain QA 1–199（199 aa）
Chain QB 1–199（199 aa）
Chain R 1–199（199 aa）
Chain SA 1–199（199 aa）
Chain SB 1–199（199 aa）
Chain T 1–199（199 aa）
Chain UA 1–199（199 aa）
Chain UB 1–199（199 aa）
Chain W 1–199（199 aa）
Chain WA 1–199（199 aa）
Chain Y 1–199（199 aa）
Chain YA 1–199（199 aa）
Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；0 mm offset with 10 sec wait time and 2-4 sec blot
Resolution 2.90 Å
6TZ4 CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (right-handed) Deposited 2019-08-10 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 72 PDB declaration: 72-meric
Chain 02 1–199（199 aa）
Chain A 1–199（199 aa）
Chain BA 1–199（199 aa）
Chain BB 1–199（199 aa）
Chain C 1–199（199 aa）
Chain DA 1–199（199 aa）
Chain DB 1–199（199 aa）
Chain E 1–199（199 aa）
Chain FA 1–199（199 aa）
Chain FB 1–199（199 aa）
Chain G 1–199（199 aa）
Chain HA 1–199（199 aa）
Chain HB 1–199（199 aa）
Chain I 1–199（199 aa）
Chain JA 1–199（199 aa）
Chain JB 1–199（199 aa）
Chain K 1–199（199 aa）
Chain LA 1–199（199 aa）
Chain LB 1–199（199 aa）
Chain M 1–199（199 aa）
Chain NA 1–199（199 aa）
Chain NB 1–199（199 aa）
Chain O 1–199（199 aa）
Chain PA 1–199（199 aa）
Chain PB 1–199（199 aa）
Chain Q 1–199（199 aa）
Chain RA 1–199（199 aa）
Chain RB 1–199（199 aa）
Chain S 1–199（199 aa）
Chain TA 1–199（199 aa）
Chain V 1–199（199 aa）
Chain VA 1–199（199 aa）
Chain X 1–199（199 aa）
Chain XA 1–199（199 aa）
Chain Z 1–199（199 aa）
Chain ZA 1–199（199 aa）
Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted with Whatman No. 1 filter paper for 4-8 seconds with a 0 mm offset at 19C and 100 percent humidity before plunging into liquid ethane
Resolution 3.20 Å
6TZ5 CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (left-handed) Deposited 2019-08-10 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 68 PDB declaration: 68-meric
Chain AA 1–199（199 aa）
Chain AB 1–199（199 aa）
Chain B 1–199（199 aa）
Chain CA 1–199（199 aa）
Chain CB 1–199（199 aa）
Chain D 1–199（199 aa）
Chain EA 1–199（199 aa）
Chain EB 1–199（199 aa）
Chain F 1–199（199 aa）
Chain GA 1–199（199 aa）
Chain GB 1–199（199 aa）
Chain H 1–199（199 aa）
Chain IA 1–199（199 aa）
Chain IB 1–199（199 aa）
Chain J 1–199（199 aa）
Chain KA 1–199（199 aa）
Chain KB 1–199（199 aa）
Chain L 1–199（199 aa）
Chain MA 1–199（199 aa）
Chain MB 1–199（199 aa）
Chain N 1–199（199 aa）
Chain OA 1–199（199 aa）
Chain OB 1–199（199 aa）
Chain P 1–199（199 aa）
Chain QA 1–199（199 aa）
Chain QB 1–199（199 aa）
Chain R 1–199（199 aa）
Chain SA 1–199（199 aa）
Chain T 1–199（199 aa）
Chain UA 1–199（199 aa）
Chain W 1–199（199 aa）
Chain WA 1–199（199 aa）
Chain Y 1–199（199 aa）
Chain YA 1–199（199 aa）
Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted with Whatman No. 1 filter paper for 4-8 seconds with a 0 mm offset at 19C and 100 percent humidity before plunging into liquid ethane
Resolution 3.10 Å
6TZ9 CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B only Deposited 2019-08-11 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 26 PDB declaration: 26-meric
Chain A 1–199（199 aa）
Chain AA 1–199（199 aa）
Chain B 1–199（199 aa）
Chain C 1–199（199 aa）
Chain D 1–199（199 aa）
Chain E 1–199（199 aa）
Chain F 1–199（199 aa）
Chain G 1–199（199 aa）
Chain H 1–199（199 aa）
Chain I 1–199（199 aa）
Chain J 1–199（199 aa）
Chain K 1–199（199 aa）
Chain L 1–199（199 aa）
Chain M 1–199（199 aa）
Chain N 1–199（199 aa）
Chain O 1–199（199 aa）
Chain P 1–199（199 aa）
Chain Q 1–199（199 aa）
Chain R 1–199（199 aa）
Chain S 1–199（199 aa）
Chain T 1–199（199 aa）
Chain V 1–199（199 aa）
Chain W 1–199（199 aa）
Chain X 1–199（199 aa）
Chain Y 1–199（199 aa）
Chain Z 1–199（199 aa）
Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted with Whatman No. 1 filter paper for 4-8 seconds with a 0 mm offset at 19C and 100 percent humidity before plunging into liquid ethane
Resolution 6.20 Å
8V2Q CHMP1B/IST1 ssRNA bound copolymer Deposited 2023-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 182 PDB declaration: 182-meric
Chain A 1–199（199 aa）
Mutation：M136V No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.95 Å
8V2R CryoEM of ssDNA bound CHMP1B/IST1 copolymer assembly Deposited 2023-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric
Chain A 1–199（199 aa）
Mutation：M136V No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.01 Å
8V2S CHMP1B/IST1 dsDNA bound copolymer Deposited 2023-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric
Chain A 1–199（199 aa）
Mutation：M136V No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.72 Å

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHM1B_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain Ab； PDBConstruct 1–160； UniProt 4–163 Author chain Ad； PDBConstruct 1–160； UniProt 4–163 Author chain Af； PDBConstruct 1–160； UniProt 4–163 Author chain Ah； PDBConstruct 1–160； UniProt 4–163 Author chain Aj； PDBConstruct 1–160； UniProt 4–163 Author chain Al； PDBConstruct 1–160； UniProt 4–163 Author chain An； PDBConstruct 1–160； UniProt 4–163 Author chain Ap； PDBConstruct 1–160； UniProt 4–163 Author chain Ar； PDBConstruct 1–160； UniProt 4–163 Author chain At； PDBConstruct 1–160； UniProt 4–163 Author chain Av； PDBConstruct 1–160； UniProt 4–163 Author chain Ax； PDBConstruct 1–160； UniProt 4–163 Author chain Az； PDBConstruct 1–160； UniProt 4–163 Author chain Bb； PDBConstruct 1–160； UniProt 4–163 Author chain Bd； PDBConstruct 1–160； UniProt 4–163 Author chain Bf； PDBConstruct 1–160； UniProt 4–163 Author chain Bh； PDBConstruct 1–160； UniProt 4–163 Author chain Bj； PDBConstruct 1–160； UniProt 4–163 Author chain Bl； PDBConstruct 1–160； UniProt 4–163 Author chain Bn； PDBConstruct 1–160； UniProt 4–163 Author chain Bp； PDBConstruct 1–160； UniProt 4–163 Author chain Br； PDBConstruct 1–160； UniProt 4–163 Author chain Bt； PDBConstruct 1–160； UniProt 4–163 Author chain Bv； PDBConstruct 1–160； UniProt 4–163 Author chain Bx； PDBConstruct 1–160； UniProt 4–163 Author chain Bz； PDBConstruct 1–160； UniProt 4–163 Author chain Cb； PDBConstruct 1–160； UniProt 4–163 Author chain Cd； PDBConstruct 1–160； UniProt 4–163 Author chain Cf； PDBConstruct 1–160； UniProt 4–163 Author chain Ch； PDBConstruct 1–160； UniProt 4–163 Author chain Cj； PDBConstruct 1–160； UniProt 4–163 Author chain Cl； PDBConstruct 1–160； UniProt 4–163 Author chain Cn； PDBConstruct 1–160； UniProt 4–163 Author chain Cp； PDBConstruct 1–160； UniProt 4–163

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.

SAXS scattering curve SAXS Profile

SAXS profile for 3jc1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3jc1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3jc1
Deposition date deposition_date2015-11-09
Structure title titleElectron cryo-microscopy of the IST1-CHMP1B ESCRT-III copolymer
Keywords keywordsESCRT-III, IST1, CHMP1B, membrane tubulation, helical filament, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier97.75 Å
Radius of gyration Rg (electron density) rg_electron96.97 Å
Forward intensity I(0) i023562000000.00
Molecular weight molecular_weight1318600.0 kDa
Excluded volume excluded_volume1657800 ų
Envelope volume envelope_volume3314100 ų
Hydration-shell volume shell_volume274540 ų
Envelope diameter envelope_diameter266.0 Å
Shell Rg shell_rg111.70 Å
Envelope Rg envelope_rg88.03 Å
Shape Rg shape_rg97.02 Å
Total Rg total_rg96.89 Å
Total atoms total_atoms92106
Residues n_residues11628
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax249.6 Å
Rg (real space) rg_real96.87 Å
Rg uncertainty (real space) rg_real_error1.26 Å
I(0) (real space) i0_real2.3560e+10
I(0) uncertainty (real space) i0_real_error4.8990e+08
Rg (reciprocal space) rg_reciprocal100.00 Å
I(0) (reciprocal space) i0_reciprocal23740000000.0000
Solution quality estimate total_estimate0.8211
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary156.0 Å
Skewness Skewness skewness-0.221
Kurtosis Kurtosis kurtosis-0.945
Angular range angular_range— – 0.0800 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2141000000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.919; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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9. Files and Curves (10)