SAXSdb — 6tz5

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

Charged multivesicular body protein 1b

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 68	IST1 homolog × 34 （P53990）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CHM1B_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain AA； PDBConstruct 1–199； UniProt 1–199 Author chain AB； PDBConstruct 1–199； UniProt 1–199 Author chain B； PDBConstruct 1–199； UniProt 1–199 Author chain CA； PDBConstruct 1–199； UniProt 1–199 Author chain CB； PDBConstruct 1–199； UniProt 1–199 Author chain D； PDBConstruct 1–199； UniProt 1–199 Author chain EA； PDBConstruct 1–199； UniProt 1–199 Author chain EB； PDBConstruct 1–199； UniProt 1–199 Author chain F； PDBConstruct 1–199； UniProt 1–199 Author chain GA； PDBConstruct 1–199； UniProt 1–199 Author chain GB； PDBConstruct 1–199； UniProt 1–199 Author chain H； PDBConstruct 1–199； UniProt 1–199 Author chain IA； PDBConstruct 1–199； UniProt 1–199 Author chain IB； PDBConstruct 1–199； UniProt 1–199 Author chain J； PDBConstruct 1–199； UniProt 1–199 Author chain KA； PDBConstruct 1–199； UniProt 1–199 Author chain KB； PDBConstruct 1–199； UniProt 1–199 Author chain L； PDBConstruct 1–199； UniProt 1–199 Author chain MA； PDBConstruct 1–199； UniProt 1–199 Author chain MB； PDBConstruct 1–199； UniProt 1–199 Author chain N； PDBConstruct 1–199； UniProt 1–199 Author chain OA； PDBConstruct 1–199； UniProt 1–199 Author chain OB； PDBConstruct 1–199； UniProt 1–199 Author chain P； PDBConstruct 1–199； UniProt 1–199 Author chain QA； PDBConstruct 1–199； UniProt 1–199 Author chain QB； PDBConstruct 1–199； UniProt 1–199 Author chain R； PDBConstruct 1–199； UniProt 1–199 Author chain SA； PDBConstruct 1–199； UniProt 1–199 Author chain T； PDBConstruct 1–199； UniProt 1–199 Author chain UA； PDBConstruct 1–199； UniProt 1–199 Author chain W； PDBConstruct 1–199； UniProt 1–199 Author chain WA； PDBConstruct 1–199； UniProt 1–199 Author chain Y； PDBConstruct 1–199； UniProt 1–199 Author chain YA； PDBConstruct 1–199； UniProt 1–199

IST1 homolog

Homo sapiens

UniProt P53990

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 68	Charged multivesicular body protein 1b × 34 （Q7LBR1）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	IST1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 1–189； UniProt 1–189 Author chain BA； PDBConstruct 1–189； UniProt 1–189 Author chain BB； PDBConstruct 1–189； UniProt 1–189 Author chain C； PDBConstruct 1–189； UniProt 1–189 Author chain DA； PDBConstruct 1–189； UniProt 1–189 Author chain DB； PDBConstruct 1–189； UniProt 1–189 Author chain E； PDBConstruct 1–189； UniProt 1–189 Author chain FA； PDBConstruct 1–189； UniProt 1–189 Author chain FB； PDBConstruct 1–189； UniProt 1–189 Author chain G； PDBConstruct 1–189； UniProt 1–189 Author chain HA； PDBConstruct 1–189； UniProt 1–189 Author chain HB； PDBConstruct 1–189； UniProt 1–189 Author chain I； PDBConstruct 1–189； UniProt 1–189 Author chain JA； PDBConstruct 1–189； UniProt 1–189 Author chain JB； PDBConstruct 1–189； UniProt 1–189 Author chain K； PDBConstruct 1–189； UniProt 1–189 Author chain LA； PDBConstruct 1–189； UniProt 1–189 Author chain LB； PDBConstruct 1–189； UniProt 1–189 Author chain M； PDBConstruct 1–189； UniProt 1–189 Author chain NA； PDBConstruct 1–189； UniProt 1–189 Author chain NB； PDBConstruct 1–189； UniProt 1–189 Author chain O； PDBConstruct 1–189； UniProt 1–189 Author chain PA； PDBConstruct 1–189； UniProt 1–189 Author chain PB； PDBConstruct 1–189； UniProt 1–189 Author chain Q； PDBConstruct 1–189； UniProt 1–189 Author chain RA； PDBConstruct 1–189； UniProt 1–189 Author chain S； PDBConstruct 1–189； UniProt 1–189 Author chain TA； PDBConstruct 1–189； UniProt 1–189 Author chain V； PDBConstruct 1–189； UniProt 1–189 Author chain VA； PDBConstruct 1–189； UniProt 1–189 Author chain X； PDBConstruct 1–189； UniProt 1–189 Author chain XA； PDBConstruct 1–189； UniProt 1–189 Author chain Z； PDBConstruct 1–189； UniProt 1–189 Author chain ZA； PDBConstruct 1–189； UniProt 1–189

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	6tz5
Deposition date deposition_date	2019-08-10
Structure title title	CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (left-handed)
Keywords keywords	membrane remodeling, membrane-bound protein filament, ESCRT-III, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

6tz5__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6tz5__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6tz5__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	99.18 Å
Rg (electron density)	98.05 Å
Total Rg	97.77 Å
Atom count	93500
Residues	12104
Excluded volume	1676000 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6tz5__assembly_1__model_1`	68-meric （68）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Charged multivesicular body protein 1b
Molecular weight formula_weight	22140.4 kDa
Mutation mutation	K37E
Source method src_method	man
Copy count entity_count	34

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	AA,AB,CB,EB,GB,IB,KB,MB,OB,QB,SA,UA,WA,YA,CA,EA,GA,IA,KA,MA,OA,QA,B,D,F,H,J,L,N,P,R,T,W,Y
Atom count atom_count	93500

MSNMEKHLFNLKFAAKELSRSAKKCDKEEKAEKAKIEKAIQKGNMEVARIHAENAIRQKNQAVNFLRMSARVDAVAARVQTAVTMGKVTKSMAGVVKSMDATLKTMNLEKISALMDKFEHQFETLDVQTQQMEDTMSSTTTLTTPQNQVDMLLQEMADEAGLDLNMELPQGQTGSVGTSVASAEQDELSQRLARLRDQV

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	IST1 homolog
Molecular weight formula_weight	21574.3 kDa
Source method src_method	man
Copy count entity_count	34

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	BB,DB,FB,HB,JB,LB,NB,PB,TA,VA,XA,ZA,BA,A,DA,FA,HA,JA,LA,NA,PA,RA,C,E,G,I,K,M,O,Q,S,V,X,Z

MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDSVVMAEAPP

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	triclinic

Resolution resolution	3.10 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	73749

CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (left-handed)

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

Charged multivesicular body protein 1b

State in the Current Structure

Other States of the Same Protein in the Database

IST1 homolog

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

6tz5__assembly_1__model_1

6tz5__assembly_1__model_1 | I(q)

6tz5__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

7. Citations (1)

CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (left-handed)

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

Charged multivesicular body protein 1b

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

IST1 homolog

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

6tz5__assembly_1__model_1

6tz5__assembly_1__model_1 | I(q)

6tz5__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

7. Citations (1)