SAXSdb — 3lk2

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

F-actin-capping protein subunit alpha-1

Gallus gallus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	F-actin-capping protein subunit beta isoforms 1 and 2 × 1 （P14315） Leucine-rich repeat-containing protein 16A × 1 （Q5VZK9） water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CAZA1_CHICK
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–286； UniProt 1–286

F-actin-capping protein subunit beta isoforms 1 and 2

Gallus gallus

UniProt P14315

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	F-actin-capping protein subunit alpha-1 × 1 （P13127） Leucine-rich repeat-containing protein 16A × 1 （Q5VZK9） water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CAPZB_CHICK
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–243； UniProt 1–243

Leucine-rich repeat-containing protein 16A

OrganismNot specified

UniProt Q5VZK9

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	F-actin-capping protein subunit alpha-1 × 1 （P13127） F-actin-capping protein subunit beta isoforms 1 and 2 × 1 （P14315） water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	LR16A_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain T； PDBConstruct 1–52； UniProt 961–1012

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	3lk2
Deposition date deposition_date	2010-01-27
Structure title title	Crystal structure of CapZ bound to the uncapping motif from CARMIL
Keywords keywords	;CapZ, CARMIL, actin filaments, uncapping, actin-filament regulators, protein-protein complex, Actin capping, Actin-binding, Cytoskeleton, PROTEIN BINDING ;; PROTEIN BINDING
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.

3lk2__assembly_1__model_1

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

Download this curve (.dat)

3lk2__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3lk2__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	27.86 Å
Rg (electron density)	27.08 Å
Total Rg	27.81 Å
Atom count	4372
Residues	545
Excluded volume	77202 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3lk2__assembly_1__model_1`	trimeric （3）	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 (4)

Entity 1 Entity 1 polymer

Description description	F-actin-capping protein subunit alpha-1
Molecular weight formula_weight	33001.8 kDa
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	4632

MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMDQFTPVKIEGYDDQVLITEHGDLGNGRFLDPRNKISFKFDHLRKEASDPQPEDTESALKQWRDACDSALRAYVKDHYPNGFCTVYGKSIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPTAQVAAVLKIQVHYYEDGNVQLVSHKDIQDSVQVSSDVQTAKEFIKIIENAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA

Source Source

Source organism organism	Gallus gallus
Common name common_name	chicken
NCBI taxonomy ID ncbi_taxonomy_id	9031
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	F-actin-capping protein subunit beta isoforms 1 and 2
Molecular weight formula_weight	27315.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLLCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYLWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNKTGSGTMNLGGSLTRQMEKDETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVNGL

Source Source

Source organism organism	Gallus gallus
Common name common_name	chicken
NCBI taxonomy ID ncbi_taxonomy_id	9031
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Leucine-rich repeat-containing protein 16A
Molecular weight formula_weight	5920.8 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	T

LRQEKRSSGFISELPSEEGKKLEHFTKLRPKRNKKQQPTQAAVCAANIVSQD

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	260

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6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d3lk2a_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.43 — Subunits of heterodimeric actin filament capping protein Capz
Superfamily Superfamily superfamily	e.43.1 — Subunits of heterodimeric actin filament capping protein Capz
Family Family family	e.43.1.1 — Capz alpha-1 subunit

CATH v4.4 (4 domains)

Domain ID domain_id	3lk2A01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1140 — Ribosomal protein S3 C-terminal domain
Homologous superfamily homologous superfamily	60 — F-actin capping protein, alpha subunit

Domain ID domain_id	3lk2A02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily	210 — F-actin capping protein, beta subunit

Domain ID domain_id	3lk2B01
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	570 — F-actin capping protein, alpha/beta subunit, N-terminal domain

Domain ID domain_id	3lk2B02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily	210 — F-actin capping protein, beta subunit

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Unit-cell length a length_a	54.900 Å
Unit-cell length b length_b	71.800 Å
Unit-cell length c length_c	154.100 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	19.710 Å
R factor r_factor	0.2150
R_work r_work	0.2090
R_free r_free	0.2680

Crystal structure of CapZ bound to the uncapping motif from CARMIL

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

F-actin-capping protein subunit alpha-1

State in the Current Structure

Other States of the Same Protein in the Database

F-actin-capping protein subunit beta isoforms 1 and 2

State in the Current Structure

Other States of the Same Protein in the Database

Leucine-rich repeat-containing protein 16A

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

3lk2__assembly_1__model_1

3lk2__assembly_1__model_1 | I(q)

3lk2__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Crystal structure of CapZ bound to the uncapping motif from CARMIL

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

F-actin-capping protein subunit alpha-1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

F-actin-capping protein subunit beta isoforms 1 and 2

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Leucine-rich repeat-containing protein 16A

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

3lk2__assembly_1__model_1

3lk2__assembly_1__model_1 | I(q)

3lk2__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

CATH v4.4 (4 domains)

7. Citations (1)