SAXSdb — 6ixp

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

Myosin-2

Saccharomyces cerevisiae

UniProt P19524

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Mitochondrial MYO2 receptor-related protein 1 × 2 （Q06324） water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Mitochondrial MYO2 receptor-related protein 1 × 2 （Q06324）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MYO2_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–421； UniProt 1152–1574 Author chain D； PDBConstruct 5–421； UniProt 1152–1574

Mitochondrial MYO2 receptor-related protein 1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt Q06324

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Myosin-2 × 1 （P19524） water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Myosin-2 × 1 （P19524）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MMR1_YEAST
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 7–39； UniProt 398–430 Author chain C； PDBConstruct 7–39； UniProt 398–430 Author chain E； PDBConstruct 7–39； UniProt 398–430 Author chain F； PDBConstruct 7–39； UniProt 398–430

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	6ixp
Deposition date deposition_date	2018-12-11
Structure title title	Structure of Myo2-GTD in complex with Mmr1
Keywords keywords	Cargo binding domain, PROTEIN BINDING, PROTEIN BINDING-CELL CYCLE complex; PROTEIN BINDING/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.

6ixp__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6ixp__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6ixp__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	28.35 Å
Rg (electron density)	28.03 Å
Total Rg	28.57 Å
Atom count	3370
Residues	420
Excluded volume	60907 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6ixp__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6ixp__assembly_2__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	Myosin-2
Molecular weight formula_weight	47961.5 kDa
Mutation mutation	Deletions 1342-1347
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D
Atom count atom_count	6796

GPGSNATQINEELYRLLEDTEILNQEITEGLLKGFEVPDAGVAIQLSKRDVVYPARILIIVLSEMWRFGLTKQSESFLAQVLTTIQKVVTQLKGNDLIPSGVFWLANVRELYSFVVFALNSILTEETFKNGMTDEEYKEYVSLVTELKDDFEALSYNIYNIWLKKLQKQLQKKAINAVVISESLPGFSAGETSGANTEEYTMDDILTFFNSIYWCMKSFHIENEVFHAVVTTLLNYVDAICFNELIMKRNFLSWKRGLQLNYNVTRLEEWCKTHGLTDGTECLQHLIQTAKLLQVRKYTIEDIDILRGICYSLTPAQLQKLISQYQVADYESPIPQEILRYVADIVKKEAALSSSGNDSKGHEHSSSIFITPETGPFTDPFSLIKTRKFDQVEAYIPAWLSLPSTKRIVDLVAQQVVQDGH

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;Baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	559292
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Mitochondrial MYO2 receptor-related protein 1
Molecular weight formula_weight	4133.6 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

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

GPGSEFGNSARIPCPKTRLARVSVLDLKKIEEQPDSSSG

Source Source

Source organism organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Common name common_name	;Baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	559292
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	4

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d6ixpa_
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.27 — DIL domain-like
Family Family family	a.118.27.1 — DIL domains from class V myosins

Domain ID domain_id	d6ixpd_
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.27 — DIL domain-like
Family Family family	a.118.27.1 — DIL domains from class V myosins

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Unit-cell length a length_a	110.387 Å
Unit-cell length b length_b	63.459 Å
Unit-cell length c length_c	169.077 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	104.72 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

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

Resolution resolution	2.733 Å
Low-resolution limit resolution_low	53.381 Å
R factor r_factor	0.2443
R_work r_work	0.2423
R_free r_free	0.2837

Structure of Myo2-GTD in complex with Mmr1

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

Myosin-2

State in the Current Structure

Other States of the Same Protein in the Database

Mitochondrial MYO2 receptor-related protein 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

6ixp__assembly_2__model_1

6ixp__assembly_2__model_1 | I(q)

6ixp__assembly_2__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 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

7. Citations (1)

Structure of Myo2-GTD in complex with Mmr1

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

Myosin-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

Mitochondrial MYO2 receptor-related protein 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

6ixp__assembly_2__model_1

6ixp__assembly_2__model_1 | I(q)

6ixp__assembly_2__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 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

7. Citations (1)