8rty

Structure of the F-actin barbed end bound by Cdc12 and profilin (ring complex) at a resolution of 6.3 Angstrom

Method: ELECTRON MICROSCOPY

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

Actin, cytoplasmic 1, N-terminally processed

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 10	Methylated-DNA--protein-cysteine methyltransferase,Cell division control protein 12 × 2 （P16455,Q10059） Phalloidin (Amanita phalloides) × 3 Profilin-1 × 1 （P07737） ADENOSINE-5'-DIPHOSPHATE × 4 MAGNESIUM ION × 4 PHOSPHATE ION × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ACTB_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–374； UniProt 2–375 Author chain B； PDBConstruct 1–374； UniProt 2–375 Author chain C； PDBConstruct 1–374； UniProt 2–375 Author chain D； PDBConstruct 1–374； UniProt 2–375

Methylated-DNA--protein-cysteine methyltransferase,Cell division control protein 12

Schizosaccharomyces pombe

UniProt P16455

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 10	Actin, cytoplasmic 1, N-terminally processed × 4 （P60709） Phalloidin (Amanita phalloides) × 3 Profilin-1 × 1 （P07737） ADENOSINE-5'-DIPHOSPHATE × 4 MAGNESIUM ION × 4 PHOSPHATE ION × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MGMT_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 5–185； UniProt 2–182 Author chain F； PDBConstruct 5–185； UniProt 2–182

Methylated-DNA--protein-cysteine methyltransferase,Cell division control protein 12

Schizosaccharomyces pombe

UniProt Q10059

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 10	Actin, cytoplasmic 1, N-terminally processed × 4 （P60709） Phalloidin (Amanita phalloides) × 3 Profilin-1 × 1 （P07737） ADENOSINE-5'-DIPHOSPHATE × 4 MAGNESIUM ION × 4 PHOSPHATE ION × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CDC12_SCHPO
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 194–703； UniProt 881–1390 Author chain F； PDBConstruct 194–703； UniProt 881–1390

Profilin-1

Homo sapiens

UniProt P07737

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 10	Actin, cytoplasmic 1, N-terminally processed × 4 （P60709） Methylated-DNA--protein-cysteine methyltransferase,Cell division control protein 12 × 2 （P16455,Q10059） Phalloidin (Amanita phalloides) × 3 ADENOSINE-5'-DIPHOSPHATE × 4 MAGNESIUM ION × 4 PHOSPHATE ION × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PROF1_HUMAN
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain P； PDBConstruct 1–139； UniProt 2–140

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	8rty
Deposition date deposition_date	2024-01-29
Structure title title	Structure of the F-actin barbed end bound by Cdc12 and profilin (ring complex) at a resolution of 6.3 Angstrom
Keywords keywords	actin, formin, Cdc12, profilin, actin assembly, STRUCTURAL PROTEIN; STRUCTURAL 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.

8rty__assembly_1__model_1

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

Download this curve (.dat)

8rty__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

8rty__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	50.29 Å
Rg (electron density)	50.20 Å
Total Rg	50.19 Å
Atom count	19260
Residues	2411
Excluded volume	342830 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`8rty__assembly_1__model_1`	decameric （10）	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 (7)

Entity 1 Entity 1 polymer

Description description	Actin, cytoplasmic 1, N-terminally processed
Molecular weight formula_weight	41632.4 kDa
Mutation mutation	C272A
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	19260

DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Trichoplusia ni

Entity 2 Entity 2 polymer

Description description	Methylated-DNA--protein-cysteine methyltransferase,Cell division control protein 12
Molecular weight formula_weight	77888.8 kDa
EC 编号 ec_number	2.1.1.63
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F

GAMADKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLLGKGTSAADAVEVPAPAAVLGGPEPLMQATAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQVLWKLLKVVKFGEVISYQQLAALAGNPAATAAVKTALSGNPVPILIPCHRVVSSSGAVGGYEGGLAVKEWLLAHEGHRLGKPGLGPAGIGAPGSNNSKITNFDIPNDATSLPTIITHPTPPPPPPLPVKTSLNTFSHPDSVNIVANDTSVAGVMPAFPPPPPPPPPLVSAAGGKFVSPAVSNNISKDDLHKTTGLTRRPTRRLKQMHWEKLNSGLEFTFWTGPSDEANKILETLHTSGVLDELDESFAMKEAKTLVKKTCARTDYMSSELQKLFGIHFHKLSHKNPNEIIRMILHCDDSMNECVEFLSSDKVLNQPKLKADLEPYRIDWANGGDLVNSEKDASELSRWDYLYVRLIVDLGGYWNQRMNALKVKNIIETNYENLVRQTKLIGRAALELRDSKVFKGLLYLILYLGNYMNDYVRQAKGFAIGSLQRLPLIKNANNTKSLLHILDITIRKHFPQFDNFSPELSTVTEAAKLNIEAIEQECSELIRGCQNLQIDCDSGALSDPTVFHPDDKILSVILPWLMEGTKKMDFLKEHLRTMNTTLNNAMRYFGEQPNDPNSKNLFFKRVDSFIIDYSKARSDNLKSEEEEASQHRRLNLVN

Source Source

Source organism organism	Schizosaccharomyces pombe
Common name common_name	fission yeast
NCBI taxonomy ID ncbi_taxonomy_id	4896
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Phalloidin (Amanita phalloides)
Molecular weight formula_weight	808.9 kDa
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

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

WXATCPA

Entity 4 Entity 4 polymer

Description description	Profilin-1
Molecular weight formula_weight	15000.2 kDa
Mutation mutation	S29C, S71M
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	P

AGWNAYIDNLMADGTCQDAAIVGYKDSPCVWAAVPGKTFVNITPAEVGVLVGKDRSSFYVNGLTLGGQKCMVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVHGGLINKKCYEMASHLRRSQY

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 5 Entity 5 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 6 Entity 6 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 7 Entity 7 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	3

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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	—

Resolution resolution	6.25 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	29092

Structure of the F-actin barbed end bound by Cdc12 and profilin (ring complex) at a resolution of 6.3 Angstrom

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

Actin, cytoplasmic 1, N-terminally processed

State in the Current Structure

Other States of the Same Protein in the Database

Methylated-DNA--protein-cysteine methyltransferase,Cell division control protein 12

State in the Current Structure

Other States of the Same Protein in the Database

Methylated-DNA--protein-cysteine methyltransferase,Cell division control protein 12

State in the Current Structure

Other States of the Same Protein in the Database

Profilin-1

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

8rty__assembly_1__model_1

8rty__assembly_1__model_1 | I(q)

8rty__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 (7)

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 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

7. Citations (1)

Structure of the F-actin barbed end bound by Cdc12 and profilin (ring complex) at a resolution of 6.3 Angstrom

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

Actin, cytoplasmic 1, N-terminally processed

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Methylated-DNA--protein-cysteine methyltransferase,Cell division control protein 12

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Methylated-DNA--protein-cysteine methyltransferase,Cell division control protein 12

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Profilin-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

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

8rty__assembly_1__model_1

8rty__assembly_1__model_1 | I(q)

8rty__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 (7)

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 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

7. Citations (1)