SAXSdb — 4d1e

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

ALPHA-ACTININ-2

HOMO SAPIENS

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 19–894	Fragment：RESIDUES 19-894 Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：0.2 M MG FORMATE 5% PEG SMEAR, 0.01 M EDTA	Resolution 3.50 Å R-free 0.258

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 4D1E	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1H8B EF-hands 3,4 from alpha-actinin / Z-repeat 7 from titin Deposited 2001-02-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 822–894（73 aa） Fragment：EF-HANDS 3&4 RESIDUE 822-894	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.6；300 K；Ionic strength (raw mmCIF value) 20；Pressure 1 NMR sample composition 0.7 MM COMPLEX	Resolution not provided
1HCI CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ Deposited 2001-05-04	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 274–746（473 aa） Fragment：SPECTRIN-LIKE REPEATS 1,2,3, AND 4 - AMINO ACIDS 274 - 746 Chain B 274–746（473 aa） Fragment：SPECTRIN-LIKE REPEATS 1,2,3, AND 4 - AMINO ACIDS 274 - 746	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；0.9 M (NH4)2SO4, 0.1 M TRISHCL PH 8.5	Resolution 2.80 Å R-free 0.295
1QUU CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ Deposited 1999-07-03	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 391–637（247 aa） Fragment：SPECTRIN-LIKE REPEATS 2 AND 3 - AMINO ACIDS 391 TO 637	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；26% PEG 400 (FLUKA), 100 MM MGSO4, 100 MM HEPES OR TRIS-HCL, pH 7.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.50 Å R-free 0.310
5A36 Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle. Deposited 2015-05-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 19–266（248 aa） Fragment：CALPONIN HOMOLOGY DOMAIN, UNP RESIDUES 19-266	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；30% POLYETHYLENE GLYCOL 1500, pH 7.5	Resolution 2.00 Å R-free 0.269
5A36 Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle. Deposited 2015-05-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 19–266（248 aa） Fragment：CALPONIN HOMOLOGY DOMAIN, UNP RESIDUES 19-266	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；30% POLYETHYLENE GLYCOL 1500, pH 7.5	Resolution 2.00 Å R-free 0.269
5A37 Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle. Deposited 2015-05-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 19–266（248 aa） Fragment：CALPONIN HOMOLOGY DOMAIN	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；28% POLYETHYLENE GLYCOL 2000, pH 7.5	Resolution 1.88 Å R-free 0.216
5A37 Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle. Deposited 2015-05-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 19–266（248 aa） Fragment：CALPONIN HOMOLOGY DOMAIN	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；28% POLYETHYLENE GLYCOL 2000, pH 7.5	Resolution 1.88 Å R-free 0.216
5A38 Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle. Deposited 2015-05-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 19–266（248 aa） Fragment：CALPONIN HOMOLOGY DOMAIN, RESIDUES 19 TO 266	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；22% POLYETHYLENE GLYCOL 3350, pH 7.5	Resolution 1.90 Å R-free 0.231
5A38 Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle. Deposited 2015-05-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 19–266（248 aa） Fragment：CALPONIN HOMOLOGY DOMAIN, RESIDUES 19 TO 266	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；22% POLYETHYLENE GLYCOL 3350, pH 7.5	Resolution 1.90 Å R-free 0.231
5A4B Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle. Deposited 2015-06-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 19–266（248 aa） Fragment：CALPONIN HOMOLOGY DOMAIN, RESIDUES 19-266	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；24% POLYETHYLENE GLYCOL 3350, pH 7.5	Resolution 2.01 Å R-free 0.235
5A4B Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle. Deposited 2015-06-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 19–266（248 aa） Fragment：CALPONIN HOMOLOGY DOMAIN, RESIDUES 19-266	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；24% POLYETHYLENE GLYCOL 3350, pH 7.5	Resolution 2.01 Å R-free 0.235
6SWT Affimer9 co-crystalised with the CH domains of alpha actinin 2. Deposited 2019-09-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 19–270（252 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；20% PEG 3350, 0.2M ammonium tartrate	Resolution 1.20 Å R-free 0.164
6TS3 EF-hands 3 and 4 of alpha-actinin in complex with CaMKII regulatory segment Deposited 2019-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 825–894（70 aa）	Not recorded	ACE ACETYL GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M BIS-TRIS pH 6.5, 25% w/v Polyethylene glycol 3,350	Resolution 1.28 Å R-free 0.199
6TS3 EF-hands 3 and 4 of alpha-actinin in complex with CaMKII regulatory segment Deposited 2019-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 825–894（70 aa）	Not recorded	ACE ACETYL GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M BIS-TRIS pH 6.5, 25% w/v Polyethylene glycol 3,350	Resolution 1.28 Å R-free 0.199
7A8T Crystal structure of sarcomeric protein FATZ-1 (mini-FATZ-1 construct) in complex with rod domain of alpha-actinin-2 Deposited 2020-08-31	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 274–746（473 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；100 mM HEPES (pH 7.0), 16% w/v Jeffamine ED-2003	Resolution 2.69 Å R-free 0.235
7A8U Crystal structure of sarcomeric protein FATZ-1 (d91-FATZ-1 construct) in complex with rod domain of alpha-actinin-2 Deposited 2020-08-31	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 274–746（473 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；100 mM Tris-HCl (pH 8.5), 200 mM trimethylamine N-oxide, 20% w/v polyethylene glycol 2,000 methyl ether	Resolution 3.80 Å R-free 0.239
7ANK Crystal structure of sarcomeric protein FATZ-1 (d91-FATZ-1 construct) in complex with half dimer of alpha-actinin-2 Deposited 2020-10-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–507（507 aa） Chain B 509–894（386 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；100 mM Bis-Tris propane (pH 7.5), 100 mM sodium citrate, 10 mM zinc chloride, 12% w/w polyethylene glycol 3,350	Resolution 3.20 Å R-free 0.284
7B55 Crystal structure of CaMKII-actinin complex bound to MES Deposited 2020-12-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 825–894（70 aa）	Not recorded	MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M MES pH 6.0, 20% w/v PEG4000, 0.2 M Lithium Sulfate	Resolution 1.60 Å R-free 0.214
7B56 Crystal structure of CaMKII-actinin complex bound to AMPPNP Deposited 2020-12-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 825–894（70 aa）	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M MES pH 6.0, 20% w/v PEG4000, 0.2 M Lithium Sulfate	Resolution 1.45 Å R-free 0.215
7B57 Crystal structure of CaMKII-actinin complex bound to ADP Deposited 2020-12-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 825–894（70 aa）	Not recorded	MG MAGNESIUM ION × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M MES pH 6.0, 20% w/v PEG4000, 0.2 M Lithium Sulfate	Resolution 1.95 Å R-free 0.247

15 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACTN2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–876； UniProt 19–894

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	4d1e
Deposition date deposition_date	2014-05-01
Structure title title	THE CRYSTAL STRUCTURE OF HUMAN MUSCLE ALPHA-ACTININ-2
Keywords keywords	CONTRACTILE PROTEIN, Z-DISC, CALMODULIN-LIKE DOMAIN, SPECTRIN DOMAIN, ACTIN BINDING DOMAIN, ABD; CONTRACTILE PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	— Å
Radius of gyration Rg (electron density) rg_electron	107.80 Å
Forward intensity I(0) i0	141901000.00
Molecular weight molecular_weight	97593.0 kDa
Excluded volume excluded_volume	121390 Å³
Envelope volume envelope_volume	286340 Å³
Hydration-shell volume shell_volume	27989 Å³
Envelope diameter envelope_diameter	328.2 Å
Shell Rg shell_rg	53.21 Å
Envelope Rg envelope_rg	106.30 Å
Shape Rg shape_rg	107.80 Å
Total Rg total_rg	106.60 Å
Total atoms total_atoms	6865
Residues n_residues	846
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	285.5 Å
Rg (real space) rg_real	98.62 Å
Rg uncertainty (real space) rg_real_error	2.22 Å
I(0) (real space) i0_real	1.3760e+08
I(0) uncertainty (real space) i0_real_error	3.1850e+06
Rg (reciprocal space) rg_reciprocal	86.27 Å
I(0) (reciprocal space) i0_reciprocal	134700000.0000
Solution quality estimate total_estimate	0.6249
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	4
Primary peak position r_peak_primary	19.0 Å
Skewness Skewness skewness	0.395
Kurtosis Kurtosis kurtosis	-1.027
Angular range angular_range	— – 0.0750 Å⁻¹
Current regularization parameter α current_alpha	0.1143
Highest regularization parameter α highest_alpha	11220000.0000
Real-space data points n_real_points	16
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.003; Stabil: 0.807; Sysdev: 1.000; Positv: 1.000; Valcen: 0.025; Smooth: 0.698

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	4d1eA04
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

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8. Citations (1)

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Unit-cell length a length_a	73.334 Å
Unit-cell length b length_b	102.613 Å
Unit-cell length c length_c	182.977 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 2 21 21
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	3.500 Å
Low-resolution limit resolution_low	51.307 Å
R factor r_factor	0.2074
R_work r_work	0.2047
R_free r_free	0.2580

Description description	ALPHA-ACTININ-2
Molecular weight formula_weight	101854.6 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	6865

THE CRYSTAL STRUCTURE OF HUMAN MUSCLE ALPHA-ACTININ-2

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

ALPHA-ACTININ-2

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	ESCHERICHIA COLI

fit	/app/data/saxs_computation/d1/4d1e/4d1e.fit
pddf	/app/data/pr_computation/d1/4d1e/4d1e.pr.out
profile	/app/data/saxs_computation/d1/4d1e/4d1e.dat