3aae

Crystal structure of Actin capping protein in complex with CARMIL fragment

Method: X-RAY DIFFRACTION

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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） 32mer peptide from Leucine-rich repeat-containing protein 16A × 1 （Q6EDY6）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	F-actin-capping protein subunit beta isoforms 1 and 2 × 1 （P14315） 32mer peptide from Leucine-rich repeat-containing protein 16A × 1 （Q6EDY6）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	F-actin-capping protein subunit beta isoforms 1 and 2 × 1 （P14315） 32mer peptide from Leucine-rich repeat-containing protein 16A × 1 （Q6EDY6）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 3	F-actin-capping protein subunit beta isoforms 1 and 2 × 1 （P14315） 32mer peptide from Leucine-rich repeat-containing protein 16A × 1 （Q6EDY6）	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 3	F-actin-capping protein subunit beta isoforms 1 and 2 × 1 （P14315） 32mer peptide from Leucine-rich repeat-containing protein 16A × 1 （Q6EDY6）	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 Author chain C； PDBConstruct 1–286； UniProt 1–286 Author chain E； PDBConstruct 1–286； UniProt 1–286 Author chain G； PDBConstruct 1–286； UniProt 1–286 Author chain I； 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） 32mer peptide from Leucine-rich repeat-containing protein 16A × 1 （Q6EDY6）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	F-actin-capping protein subunit alpha-1 × 1 （P13127） 32mer peptide from Leucine-rich repeat-containing protein 16A × 1 （Q6EDY6）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	F-actin-capping protein subunit alpha-1 × 1 （P13127） 32mer peptide from Leucine-rich repeat-containing protein 16A × 1 （Q6EDY6）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 3	F-actin-capping protein subunit alpha-1 × 1 （P13127） 32mer peptide from Leucine-rich repeat-containing protein 16A × 1 （Q6EDY6）	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 3	F-actin-capping protein subunit alpha-1 × 1 （P13127） 32mer peptide from Leucine-rich repeat-containing protein 16A × 1 （Q6EDY6）	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 1–277； UniProt 1–277 Author chain D； PDBConstruct 1–277； UniProt 1–277 Author chain F； PDBConstruct 1–277； UniProt 1–277 Author chain H； PDBConstruct 1–277； UniProt 1–277 Author chain J； PDBConstruct 1–277； UniProt 1–277

32mer peptide from Leucine-rich repeat-containing protein 16A

Mus musculus

UniProt Q6EDY6

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）	Consistent with protein count
2	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）	Consistent with protein count
3	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）	Consistent with protein count
4	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）	Consistent with protein count
5	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）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	LR16A_MOUSE
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain V； PDBConstruct 6–37； UniProt 971–1002 Author chain W； PDBConstruct 6–37； UniProt 971–1002 Author chain X； PDBConstruct 6–37； UniProt 971–1002 Author chain Y； PDBConstruct 6–37； UniProt 971–1002 Author chain Z； PDBConstruct 6–37； UniProt 971–1002

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	3aae
Deposition date deposition_date	2009-11-16
Structure title title	Crystal structure of Actin capping protein in complex with CARMIL fragment
Keywords keywords	;ACTIN CAPPING PROTEIN, BARBED END REGULATION, CARMIL FAMILY PROTEIN, CONFORMATIONAL CHANGE, CELL MOTILITY, Actin capping, Actin-binding, Cytoskeleton, Isopeptide bond, Leucine-rich repeat, 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.

3aae__assembly_1__model_1

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

Download this curve (.dat)

3aae__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3aae__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.06 Å
Rg (electron density)	27.28 Å
Total Rg	28.03 Å
Atom count	4533
Residues	563
Excluded volume	80043 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3aae__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3aae__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3aae__assembly_3__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`3aae__assembly_4__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`3aae__assembly_5__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 (3)

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	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G,I
Atom count atom_count	22177

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	31403.4 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F,H,J

MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLLCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYLWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNKTGSGTMNLGGSLTRQMEKDETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVNGLRSIDAIPDNQKYKQLQRELSQVLTQRQIYIQPDN

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	32mer peptide from Leucine-rich repeat-containing protein 16A
Molecular weight formula_weight	4167.8 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	X,Y,Z,W,V

GPLGSSSGLISELPSEEGRRLEHFTKLRPKRNKKQQP

Source Source

Source organism organism	Mus musculus
Common name common_name	mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090
Host organism host_organism	Escherichia coli

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6. Fold Classification (SCOP + CATH) 20 domains

CATH v4.4 (20 domains)

Domain ID domain_id	3aaeA01
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	3aaeA02
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	3aaeB01
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	3aaeB02
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	3aaeC01
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	3aaeC02
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	3aaeD01
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	3aaeD02
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	3aaeE01
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	3aaeE02
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	3aaeF01
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	3aaeF02
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	3aaeG01
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	3aaeG02
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	3aaeH01
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	3aaeH02
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	3aaeI01
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	3aaeI02
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	3aaeJ01
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	3aaeJ02
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	231.153 Å
Unit-cell length b length_b	104.358 Å
Unit-cell length c length_c	186.633 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	119.09 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	20

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	3.300 Å
Low-resolution limit resolution_low	49.700 Å
R factor r_factor	0.2447
R_work r_work	0.2433
R_free r_free	0.2709

Crystal structure of Actin capping protein in complex with CARMIL fragment

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

32mer peptide from 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

3aae__assembly_1__model_1

3aae__assembly_1__model_1 | I(q)

3aae__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 (3)

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

Source Source

6. Fold Classification (SCOP + CATH) 20 domains

CATH v4.4 (20 domains)

7. Citations (1)

Crystal structure of Actin capping protein in complex with CARMIL fragment

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

32mer peptide from 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

3aae__assembly_1__model_1

3aae__assembly_1__model_1 | I(q)

3aae__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 (3)

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

Source Source

6. Fold Classification (SCOP + CATH) 20 domains

CATH v4.4 (20 domains)

7. Citations (1)