SAXSdb — 3eab

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

Spastin

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	CHMP1b × 1 （B2RA72）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	CHMP1b × 1 （B2RA72）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	CHMP1b × 1 （B2RA72）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	CHMP1b × 1 （B2RA72）	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	CHMP1b × 1 （B2RA72）	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	CHMP1b × 1 （B2RA72）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SPAST_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–89； UniProt 112–196 Author chain B； PDBConstruct 5–89； UniProt 112–196 Author chain C； PDBConstruct 5–89； UniProt 112–196 Author chain D； PDBConstruct 5–89； UniProt 112–196 Author chain E； PDBConstruct 5–89； UniProt 112–196 Author chain F； PDBConstruct 5–89； UniProt 112–196

CHMP1b

Homo sapiens

UniProt B2RA72

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Spastin × 1 （Q9UBP0）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Spastin × 1 （Q9UBP0）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Spastin × 1 （Q9UBP0）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Spastin × 1 （Q9UBP0）	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	Spastin × 1 （Q9UBP0）	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	Spastin × 1 （Q9UBP0）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	B2RA72_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain G； PDBConstruct 1–50； UniProt 145–194 Author chain H； PDBConstruct 1–50； UniProt 145–194 Author chain I； PDBConstruct 1–50； UniProt 145–194 Author chain J； PDBConstruct 1–50； UniProt 145–194 Author chain K； PDBConstruct 1–50； UniProt 145–194 Author chain L； PDBConstruct 1–50； UniProt 145–194

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	3eab
Deposition date deposition_date	2008-08-25
Structure title title	Crystal structure of Spastin MIT in complex with ESCRT III
Keywords keywords	;Spastin, CHMP, MIT, ESCRT, Alternative splicing, ATP-binding, Cytoplasm, Disease mutation, Hereditary spastic paraplegia, Nucleotide-binding, Nucleus, Polymorphism, CELL CYCLE ;; CELL CYCLE
Experimental Method method	X-RAY DIFFRACTION

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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.

3eab__assembly_1__model_1

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

Download this curve (.dat)

3eab__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3eab__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	16.05 Å
Rg (electron density)	15.04 Å
Total Rg	16.29 Å
Atom count	1016
Residues	129
Excluded volume	18013 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3eab__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3eab__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3eab__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`3eab__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`3eab__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`3eab__assembly_6__model_1`	dimeric （2）	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	Spastin
Molecular weight formula_weight	10314.9 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	5977

MGSMEAERVRVFHKQAFEYISIALRIDEDEKAGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLE

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	CHMP1b
Molecular weight formula_weight	5420.9 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,H,I,J,K,L

QVDMLLQEMADEAGLDLNMELPQGQTGSVGTSVASAEQDELSQRLARLRD

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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6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id	3eabA01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	80 — Phosphotransferase system, lactose/cellobiose-type IIA subunit

Domain ID domain_id	3eabB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	80 — Phosphotransferase system, lactose/cellobiose-type IIA subunit

Domain ID domain_id	3eabC01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	80 — Phosphotransferase system, lactose/cellobiose-type IIA subunit

Domain ID domain_id	3eabD01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	80 — Phosphotransferase system, lactose/cellobiose-type IIA subunit

Domain ID domain_id	3eabE00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	80 — Phosphotransferase system, lactose/cellobiose-type IIA subunit

Domain ID domain_id	3eabF01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	80 — Phosphotransferase system, lactose/cellobiose-type IIA subunit

Domain ID domain_id	3eabG00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	440 —

Domain ID domain_id	3eabI00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	440 —

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Unit-cell length a length_a	151.967 Å
Unit-cell length b length_b	95.493 Å
Unit-cell length c length_c	100.360 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	24

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	47.650 Å
R factor r_factor	0.2320
R_work r_work	0.2320
R_free r_free	0.2680

Crystal structure of Spastin MIT in complex with ESCRT III

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

Spastin

State in the Current Structure

Other States of the Same Protein in the Database

CHMP1b

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

3eab__assembly_1__model_1

3eab__assembly_1__model_1 | I(q)

3eab__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

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

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)

Crystal structure of Spastin MIT in complex with ESCRT III

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

Spastin

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

CHMP1b

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

3eab__assembly_1__model_1

3eab__assembly_1__model_1 | I(q)

3eab__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

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

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)