SAXSdb — 4gdo

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

Plectin

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 1492–1530 Chain B； UniProt 1492–1530	Fragment：FRAGMENT OF THE ROD DOMAIN, UNP residues 1492-1530	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 4.5；298 K；0.1M sodium acetate, 2.2M sodium chloride, 0.2M lithium sulfate, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 1.70 Å R-free 0.248
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1492–1530 Chain D； UniProt 1492–1530	Fragment：FRAGMENT OF THE ROD DOMAIN, UNP residues 1492-1530	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 4.5；298 K；0.1M sodium acetate, 2.2M sodium chloride, 0.2M lithium sulfate, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 1.70 Å R-free 0.248
3	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 1492–1530 Chain F； UniProt 1492–1530	Fragment：FRAGMENT OF THE ROD DOMAIN, UNP residues 1492-1530	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 4.5；298 K；0.1M sodium acetate, 2.2M sodium chloride, 0.2M lithium sulfate, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 1.70 Å R-free 0.248

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 4GDO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1MB8 Crystal Structure of the actin binding domain of plectin Deposited 2002-08-02	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 59–293（235 aa） Fragment：Residues 59-293	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.15 Å R-free 0.261
2N03 Solution NMR Structure plectin repeat domain 6 (4403-4606) of Plectin from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR6354E Deposited 2015-03-04	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 4403–4606（204 aa） Fragment：residues 4403-4606	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 100；Pressure ambient NMR sample composition 1 mM [U-100% 13C; U-100% 15N; U-2H; ILV-1H] protein, 20 mM MES, 100 mM NaCl, 5 mM CaCl2, 10 mM DTT, 0.02 mM NaN3, 50 uM DSS, 1 ratio protease inhibitor, 90/10 % H2O/D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-100% 13C; U-100% 15N] protein, 20 mM MES, 100 mM NaCl, 5 mM CaCl2, 10 mM DTT, 0.02 mM NaN3, 50 uM DSS, 1 ratio protease inhibitor, 90/10 % H2O/D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-5% 13C; U-100% 15N] protein, 20 mM MES, 100 mM NaCl, 5 mM CaCl2, 10 mM DTT, 0.02 mM NaN3, 50 uM DSS, 1 ratio protease inhibitor, 90/10 % H2O/D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
3F7P Crystal structure of a complex between integrin beta4 and plectin Deposited 2008-11-10	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 1–293（293 aa） Fragment：Actin-binding domain, residues 1-293	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.8；298 K；0.1M Sodium Acetate, 0.2M CaCl2, 10% PEG 6000, pH 5.8, VAPOR DIFFUSION, temperature 298K	Resolution 2.75 Å R-free 0.257
3F7P Crystal structure of a complex between integrin beta4 and plectin Deposited 2008-11-10	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 1–293（293 aa） Fragment：Actin-binding domain, residues 1-293	Not recorded	EDO 1,2-ETHANEDIOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.8；298 K；0.1M Sodium Acetate, 0.2M CaCl2, 10% PEG 6000, pH 5.8, VAPOR DIFFUSION, temperature 298K	Resolution 2.75 Å R-free 0.257
3PDY Structure of the third and fourth spectrin repeats of the plakin domain of plectin Deposited 2010-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 653–858（206 aa） Fragment：SPECTRIN REPEATS 3 AND 4 (UNP Residues 653-848)	Not recorded	EDO 1,2-ETHANEDIOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；297 K；0.1M HEPES, 17% PEG 4000, 8% ISOPROPANOL, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 297K	Resolution 2.22 Å R-free 0.248
3PDY Structure of the third and fourth spectrin repeats of the plakin domain of plectin Deposited 2010-10-25	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 653–858（206 aa） Fragment：SPECTRIN REPEATS 3 AND 4 (UNP Residues 653-848)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；297 K；0.1M HEPES, 17% PEG 4000, 8% ISOPROPANOL, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 297K	Resolution 2.22 Å R-free 0.248
3PDY Structure of the third and fourth spectrin repeats of the plakin domain of plectin Deposited 2010-10-25	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 653–858（206 aa） Fragment：SPECTRIN REPEATS 3 AND 4 (UNP Residues 653-848) Chain B 653–858（206 aa） Fragment：SPECTRIN REPEATS 3 AND 4 (UNP Residues 653-848)	Not recorded	EDO 1,2-ETHANEDIOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；297 K；0.1M HEPES, 17% PEG 4000, 8% ISOPROPANOL, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 297K	Resolution 2.22 Å R-free 0.248
3PE0 Structure of the central region of the plakin domain of plectin Deposited 2010-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 750–1028（279 aa） Fragment：SPECTRIN REPEATS 4 AND 5, SH3 (UNP Residues 747-918)	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.2；277 K；0.1 M imidazole, 0.2 M calcium acetate, 9% PEG 8000, 2 mM DTT, pH 7.2, VAPOR DIFFUSION, temperature 277K	Resolution 2.95 Å R-free 0.265
3PE0 Structure of the central region of the plakin domain of plectin Deposited 2010-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 750–1028（279 aa） Fragment：SPECTRIN REPEATS 4 AND 5, SH3 (UNP Residues 747-918)	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.2；277 K；0.1 M imidazole, 0.2 M calcium acetate, 9% PEG 8000, 2 mM DTT, pH 7.2, VAPOR DIFFUSION, temperature 277K	Resolution 2.95 Å R-free 0.265
4Q58 Crystal structure of the plectin 1a actin-binding domain/integrin beta 4 fragment complex Deposited 2014-04-16	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 175–400（226 aa） Fragment：actin-binding domain (UNP residues 175-400)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；295 K；20 mM HEPES, pH 6.5, 150 mM sodium formate, 7.5% PEG550 MME, 3% sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 4.00 Å R-free 0.287
4Q58 Crystal structure of the plectin 1a actin-binding domain/integrin beta 4 fragment complex Deposited 2014-04-16	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 175–400（226 aa） Fragment：actin-binding domain (UNP residues 175-400)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；295 K；20 mM HEPES, pH 6.5, 150 mM sodium formate, 7.5% PEG550 MME, 3% sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 4.00 Å R-free 0.287
4Q59 Crystal structure of plectin 1a actin-binding domain Deposited 2014-04-16	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 175–400（226 aa） Fragment：actin-binding domain (UNP residues 175-400)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；0.05 M potassium phosphate monobasic, 20% PEG8000, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.30 Å R-free 0.245
4Q59 Crystal structure of plectin 1a actin-binding domain Deposited 2014-04-16	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 175–400（226 aa） Fragment：actin-binding domain (UNP residues 175-400)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；0.05 M potassium phosphate monobasic, 20% PEG8000, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.30 Å R-free 0.245
5J1F Structure of the spectrin repeats 5 and 6 of the plakin domain of plectin Deposited 2016-03-29	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 860–928（69 aa） Chain A 999–1116（118 aa）	Mutation：F752A,F752A Mutation：F752A,F752A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；A protein solution at 30 mg/ml in 10 mM Tris-Hcl (pH 7.5), 50 mM NaCl, 1 mM DTT was mixed with an equal volume of crystallization solution 0.1 M Bis-Tris-Propane (pH 6.0), 18% PEG 3350, 0.2 Na malonate	Resolution 3.00 Å R-free 0.277
5J1F Structure of the spectrin repeats 5 and 6 of the plakin domain of plectin Deposited 2016-03-29	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 860–928（69 aa） Chain B 999–1116（118 aa）	Mutation：F752A,F752A Mutation：F752A,F752A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；A protein solution at 30 mg/ml in 10 mM Tris-Hcl (pH 7.5), 50 mM NaCl, 1 mM DTT was mixed with an equal volume of crystallization solution 0.1 M Bis-Tris-Propane (pH 6.0), 18% PEG 3350, 0.2 Na malonate	Resolution 3.00 Å R-free 0.277
5J1G Structure of the spectrin repeats 7 and 8 of the plakin domain of plectin Deposited 2016-03-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1004–1233（230 aa） Fragment：UNP residues 1004-1233	Not recorded	1PE PENTAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.7；298 K；A protein solution at 27 mg/ml in 10 mM Tris-HCl (pH 7.5), 50 mM NaCl was mixed with an equal volume of crystallization solution 50 mM Tris-HCl (pH 7.7), 0.2 M NaF, 18% PEG 3350	Resolution 1.80 Å R-free 0.218
5J1G Structure of the spectrin repeats 7 and 8 of the plakin domain of plectin Deposited 2016-03-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1004–1233（230 aa） Fragment：UNP residues 1004-1233	Not recorded	1PE PENTAETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.7；298 K；A protein solution at 27 mg/ml in 10 mM Tris-HCl (pH 7.5), 50 mM NaCl was mixed with an equal volume of crystallization solution 50 mM Tris-HCl (pH 7.7), 0.2 M NaF, 18% PEG 3350	Resolution 1.80 Å R-free 0.218
5J1H Structure of the spectrin repeats 5 and 6 of the plakin domain of plectin Deposited 2016-03-29	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 860–928（69 aa） Chain A 999–1116（118 aa）	Mutation：F752A,F752A Mutation：F752A,F752A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；Protein at 30 mg/ml in 10 mM Tris-HCl (pH 7.5), 50 mM NaCl, 1 mM DTT was mixed with an equal volume of the crystallization solution 0.2 M Na/K tartrate, 20% PEG3350	Resolution 2.80 Å R-free 0.269
5J1H Structure of the spectrin repeats 5 and 6 of the plakin domain of plectin Deposited 2016-03-29	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 860–928（69 aa） Chain B 999–1116（118 aa）	Mutation：F752A,F752A Mutation：F752A,F752A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；Protein at 30 mg/ml in 10 mM Tris-HCl (pH 7.5), 50 mM NaCl, 1 mM DTT was mixed with an equal volume of the crystallization solution 0.2 M Na/K tartrate, 20% PEG3350	Resolution 2.80 Å R-free 0.269
5J1I Structure of the spectrin repeats 7, 8, and 9 of the plakin domain of plectin Deposited 2016-03-29	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 1004–1372（369 aa） Fragment：UNP residues 1104-1372	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；Protein solution at 12 mg/ml in 10 mM Tris-HCl (pH 7.5), 50 mM NaCl, 1 mM DTT was mixed with crystallization solution 0.1 M Bis-Tris-propane (pH 8.0), 16% PEG 3350, 0.3 M Na/K tartrate	Resolution 2.80 Å R-free 0.322
5J1I Structure of the spectrin repeats 7, 8, and 9 of the plakin domain of plectin Deposited 2016-03-29	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 1004–1372（369 aa） Fragment：UNP residues 1104-1372	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；Protein solution at 12 mg/ml in 10 mM Tris-HCl (pH 7.5), 50 mM NaCl, 1 mM DTT was mixed with crystallization solution 0.1 M Bis-Tris-propane (pH 8.0), 16% PEG 3350, 0.3 M Na/K tartrate	Resolution 2.80 Å R-free 0.322

11 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PLEC_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–43； UniProt 1492–1530 Author chain B； PDBConstruct 5–43； UniProt 1492–1530 Author chain C； PDBConstruct 5–43； UniProt 1492–1530 Author chain D； PDBConstruct 5–43； UniProt 1492–1530 Author chain E； PDBConstruct 5–43； UniProt 1492–1530 Author chain F； PDBConstruct 5–43； UniProt 1492–1530

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	4gdo
Deposition date deposition_date	2012-08-01
Structure title title	Structure of a fragment of the rod domain of plectin
Keywords keywords	COILED-COIL, STRUCTURAL PROTEIN; STRUCTURAL 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	27.88 Å
Radius of gyration Rg (electron density) rg_electron	28.83 Å
Forward intensity I(0) i0	11853800.00
Molecular weight molecular_weight	23532.0 kDa
Excluded volume excluded_volume	28496 Å³
Envelope volume envelope_volume	40239 Å³
Hydration-shell volume shell_volume	14860 Å³
Envelope diameter envelope_diameter	119.6 Å
Shell Rg shell_rg	28.17 Å
Envelope Rg envelope_rg	30.20 Å
Shape Rg shape_rg	28.84 Å
Total Rg total_rg	28.73 Å
Total atoms total_atoms	3247
Residues n_residues	223
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	113.9 Å
Rg (real space) rg_real	28.87 Å
Rg uncertainty (real space) rg_real_error	1.65 Å
I(0) (real space) i0_real	1.1850e+07
I(0) uncertainty (real space) i0_real_error	1.9860e+05
Rg (reciprocal space) rg_reciprocal	28.56 Å
I(0) (reciprocal space) i0_reciprocal	11850000.0000
Solution quality estimate total_estimate	0.6573
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.0 Å
Skewness Skewness skewness	0.859
Kurtosis Kurtosis kurtosis	0.302
Angular range angular_range	— – 0.2850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	915200.0000
Real-space data points n_real_points	58
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.190; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.020; Smooth: 0.951

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	4gdoA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	580 — Single Helix bin

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8. Citations (1)

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Unit-cell length a length_a	90.620 Å
Unit-cell length b length_b	35.870 Å
Unit-cell length c length_c	75.690 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	94.11 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	24

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

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	45.194 Å
R factor r_factor	0.2148
R_work r_work	0.2127
R_free r_free	0.2484

Description description	Plectin
Molecular weight formula_weight	4880.4 kDa
Source method src_method	man
Copy count entity_count	6

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	3410

Structure of a fragment of the rod domain of plectin

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

Plectin

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

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

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	163

fit	/app/data/saxs_computation/gd/4gdo/4gdo.fit
pddf	/app/data/pr_computation/gd/4gdo/4gdo.pr.out
profile	/app/data/saxs_computation/gd/4gdo/4gdo.dat