SAXSdb — 1pxy

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

fimbrin-like protein

Arabidopsis thaliana

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FIMB1_ARATH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–506； UniProt 123–623 Author chain B； PDBConstruct 6–506； UniProt 123–623

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	1pxy
Deposition date deposition_date	2003-07-07
Structure title title	Crystal structure of the actin-crosslinking core of Arabidopsis fimbrin
Keywords keywords	;CALPONIN HOMOLOGY, F-ACTIN-BINDING DOMAIN (ABD), F-ACTIN-CROSSLINKING, Structural Genomics, PSI, Protein Structure Initiative, New York SGX Research Center for Structural Genomics, NYSGXRC, STRUCTURAL PROTEIN ;; STRUCTURAL PROTEIN
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.

1pxy__assembly_1__model_1

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

Download this curve (.dat)

1pxy__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1pxy__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	26.23 Å
Rg (electron density)	25.16 Å
Total Rg	26.00 Å
Atom count	3725
Residues	465
Excluded volume	67142 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1pxy__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1pxy__assembly_2__model_1`	monomeric （1）	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	fimbrin-like protein
Molecular weight formula_weight	57547.6 kDa
Mutation mutation	V240L
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	7708

GSPGIQSEKGPFVQHINRYLGDDPFLKQFLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLNSAKAVGCSVVNIGTQDLAEGRPHLVLGLISQLIKIQLLADLNLKKTPQLVELLEDSDDVEELLRLPPEKVLLKWMNFHLKKGGYKKTVSNFSADLKDAQAYAFLLNVLAPEHCDPATLDAKDPLERAELVLSHAERMNCKRYLTAEEIVEGSSTLNLAFVAQIFHERNGLNKDGKYAFAEMMTEDVETCRDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMPFRKVENCNQVIKIGKQLKFSLVNVAGNDIVQGNKKLILGLLWQLMRFHMLQLLKSLRSRTLGKEMTDADILSWANRKVRTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNATYIVSVARKLGCSVFLLPEDIVEVNQKMILILTASIMYWSLQR

Source Source

Source organism organism	Arabidopsis thaliana
Common name common_name	thale cress
NCBI taxonomy ID ncbi_taxonomy_id	3702
Host organism host_organism	Escherichia coli BL21

Entity 2 Entity 2 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	190

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1pxya_
Class class	a — All alpha proteins
Fold Fold fold	a.40 — CH domain-like
Superfamily Superfamily superfamily	a.40.1 — Calponin-homology domain, CH-domain
Family Family family	a.40.1.1 — Calponin-homology domain, CH-domain

Domain ID domain_id	d1pxyb_
Class class	a — All alpha proteins
Fold Fold fold	a.40 — CH domain-like
Superfamily Superfamily superfamily	a.40.1 — Calponin-homology domain, CH-domain
Family Family family	a.40.1.1 — Calponin-homology domain, CH-domain

CATH v4.4 (8 domains)

Domain ID domain_id	1pxyA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	10 — Calponin-like domain

Domain ID domain_id	1pxyA02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	10 — Calponin-like domain

Domain ID domain_id	1pxyA03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	10 — Calponin-like domain

Domain ID domain_id	1pxyA04
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	10 — Calponin-like domain

Domain ID domain_id	1pxyB01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	10 — Calponin-like domain

Domain ID domain_id	1pxyB02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	10 — Calponin-like domain

Domain ID domain_id	1pxyB03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	10 — Calponin-like domain

Domain ID domain_id	1pxyB04
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	10 — Calponin-like domain

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Unit-cell length a length_a	62.688 Å
Unit-cell length b length_b	104.981 Å
Unit-cell length c length_c	104.411 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.93 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2293
R_work r_work	0.2293
R_free r_free	0.2699

Crystal structure of the actin-crosslinking core of Arabidopsis fimbrin

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

fimbrin-like protein

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

1pxy__assembly_1__model_1

1pxy__assembly_1__model_1 | I(q)

1pxy__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 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (2 domains)

CATH v4.4 (8 domains)

7. Citations (1)

Crystal structure of the actin-crosslinking core of Arabidopsis fimbrin

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

fimbrin-like protein

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

1pxy__assembly_1__model_1

1pxy__assembly_1__model_1 | I(q)

1pxy__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 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (2 domains)

CATH v4.4 (8 domains)

7. Citations (1)