SAXSdb — 6uui

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

Keratin, type II cytoskeletal 1

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 370–489	Fragment：2B domain	Keratin, type I cytoskeletal 10 × 1 （P13645） BOG octyl beta-D-glucopyranoside × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.4；285.15 K；Ammonium phosphate dibasic, Tris, N-octyl-B-D-glucoside	Resolution 2.07 Å R-free 0.277

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 6UUI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4ZRY Crystal structure of the heterocomplex between coil 2B domains of human intermediate filament proteins keratin 1 (KRT1) and keratin 10 (KRT10) Deposited 2015-05-12	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 370–489（120 aa） Fragment：coil 2B domain (UNP residues 370-489)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298.15 K；0.1 M HEPES, 2.0 M ammonium formate	Resolution 3.30 Å R-free 0.277
4ZRY Crystal structure of the heterocomplex between coil 2B domains of human intermediate filament proteins keratin 1 (KRT1) and keratin 10 (KRT10) Deposited 2015-05-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 370–489（120 aa） Fragment：coil 2B domain (UNP residues 370-489)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298.15 K；0.1 M HEPES, 2.0 M ammonium formate	Resolution 3.30 Å R-free 0.277
6E2J Crystal structure of the heterocomplex between human keratin 1 coil 1B containing S233L mutation and wild-type human keratin 10 coil 1B Deposited 2018-07-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 226–331（106 aa）	Mutation：S233L	SO4 SULFATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；0.1 M Tris, 1.5 M ammonium sulfate, 12% glycerol	Resolution 2.39 Å R-free 0.294
6E2J Crystal structure of the heterocomplex between human keratin 1 coil 1B containing S233L mutation and wild-type human keratin 10 coil 1B Deposited 2018-07-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 226–331（106 aa）	Mutation：S233L	SO4 SULFATE ION × 16	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；0.1 M Tris, 1.5 M ammonium sulfate, 12% glycerol	Resolution 2.39 Å R-free 0.294

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	K2C1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain C； PDBConstruct 1–120； UniProt 370–489

Keratin, type I cytoskeletal 10

Homo sapiens

UniProt P13645

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain X； UniProt 337–456	Fragment：2B domain Mutation：C401A	Keratin, type II cytoskeletal 1 × 1 （P04264） BOG octyl beta-D-glucopyranoside × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.4；285.15 K；Ammonium phosphate dibasic, Tris, N-octyl-B-D-glucoside	Resolution 2.07 Å R-free 0.277

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 6UUI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3ASW Structural and biochemical characterization of ClfB:ligand interactions Deposited 2010-12-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 473–487（15 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；0.9M sodium citrate, 90mM imidazole pH 8.0 , VAPOR DIFFUSION, temperature 298K	Resolution 2.60 Å R-free 0.219
4F1Z Crystal structures reveal the multi-ligand binding mechanism of the Staphylococcus aureus ClfB Deposited 2012-05-07	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain Q 473–486（14 aa） Fragment：tail region, UNP residues 473-486	Not recorded	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；291 K；0.1M sodium citrate tribasic dehydrate, 20% 2-propanol, 20% PEG 4000, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.30 Å R-free 0.251
4ZRY Crystal structure of the heterocomplex between coil 2B domains of human intermediate filament proteins keratin 1 (KRT1) and keratin 10 (KRT10) Deposited 2015-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 337–456（120 aa） Fragment：coil 2B domain (UNP residues 337-456)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298.15 K；0.1 M HEPES, 2.0 M ammonium formate	Resolution 3.30 Å R-free 0.277
4ZRY Crystal structure of the heterocomplex between coil 2B domains of human intermediate filament proteins keratin 1 (KRT1) and keratin 10 (KRT10) Deposited 2015-05-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 337–456（120 aa） Fragment：coil 2B domain (UNP residues 337-456)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298.15 K；0.1 M HEPES, 2.0 M ammonium formate	Resolution 3.30 Å R-free 0.277
6E2J Crystal structure of the heterocomplex between human keratin 1 coil 1B containing S233L mutation and wild-type human keratin 10 coil 1B Deposited 2018-07-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 195–296（102 aa）	Not recorded	SO4 SULFATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；0.1 M Tris, 1.5 M ammonium sulfate, 12% glycerol	Resolution 2.39 Å R-free 0.294
6E2J Crystal structure of the heterocomplex between human keratin 1 coil 1B containing S233L mutation and wild-type human keratin 10 coil 1B Deposited 2018-07-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 195–296（102 aa）	Not recorded	SO4 SULFATE ION × 16	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；0.1 M Tris, 1.5 M ammonium sulfate, 12% glycerol	Resolution 2.39 Å R-free 0.294
6EC0 Crystal structure of the wild-type heterocomplex between coil 1B domains of human intermediate filament proteins keratin 1 (KRT1) and keratin 10 (KRT10) Deposited 2018-08-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 195–296（102 aa）	Not recorded	CD CADMIUM ION × 8 CO COBALT (II) ION × 4 NI NICKEL (II) ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298 K；11% PEG 3350, 0.1 M HEPES, 5 mM cobalt chloride, 5 mM cadmium chloride, 5 mM magnesium chloride, 5 mM nickel chloride	Resolution 2.98 Å R-free 0.300

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	K1C10_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain X； PDBConstruct 3–122； UniProt 337–456

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	6uui
Deposition date deposition_date	2019-10-30
Structure title title	Crystal structure of the heterocomplex between coil 2B domains of wild-type keratin 1 (KRT1) and keratin 10 (KRT10) containing mutation Cys401Ala
Keywords keywords	intermediate filament, cytoskeleton, skin, coiled-coil, PROTEIN FIBRIL; PROTEIN FIBRIL
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	43.92 Å
Radius of gyration Rg (electron density) rg_electron	46.13 Å
Forward intensity I(0) i0	10932000.00
Molecular weight molecular_weight	25040.0 kDa
Excluded volume excluded_volume	31002 Å³
Envelope volume envelope_volume	49294 Å³
Hydration-shell volume shell_volume	12057 Å³
Envelope diameter envelope_diameter	162.8 Å
Shell Rg shell_rg	34.26 Å
Envelope Rg envelope_rg	47.98 Å
Shape Rg shape_rg	46.16 Å
Total Rg total_rg	45.19 Å
Total atoms total_atoms	3525
Residues n_residues	215
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	170.8 Å
Rg (real space) rg_real	45.27 Å
Rg uncertainty (real space) rg_real_error	3.57 Å
I(0) (real space) i0_real	1.0930e+07
I(0) uncertainty (real space) i0_real_error	2.3570e+05
Rg (reciprocal space) rg_reciprocal	43.93 Å
I(0) (reciprocal space) i0_reciprocal	10910000.0000
Solution quality estimate total_estimate	0.5417
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	19.0 Å
Skewness Skewness skewness	0.642
Kurtosis Kurtosis kurtosis	-0.475
Angular range angular_range	— – 0.1800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	476400.0000
Real-space data points n_real_points	37
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.011; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.006; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Keratin, type II cytoskeletal 1
Molecular weight formula_weight	13850.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C
Atom count atom_count	3678

ESLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGE

来源 Source

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 BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Keratin, type I cytoskeletal 10
Molecular weight formula_weight	14102.5 kDa
Mutation mutation	C401A
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	X

GSEAWFNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRYAVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLEGE

来源 Source

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 BL21(DE3)

Entity 3 Entity 3 non-polymer

Description description	octyl beta-D-glucopyranoside
Molecular weight formula_weight	292.4 kDa
Source method src_method	man
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	107

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d6uuic_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.20 — Intermediate filament protein, coiled coil region
Family Family family	h.1.20.0 — automated matches

Domain ID domain_id	d6uuix_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.20 — Intermediate filament protein, coiled coil region
Family Family family	h.1.20.0 — automated matches

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8. Citations (1)

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Unit-cell length a length_a	100.124 Å
Unit-cell length b length_b	100.124 Å
Unit-cell length c length_c	224.788 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 61 2 2
Space-group number int_tables_number	178
Crystal system crystal_system	—

Resolution resolution	2.069 Å
Low-resolution limit resolution_low	48.865 Å
R factor r_factor	0.2517
R_work r_work	0.2503
R_free r_free	0.2769

fit	/app/data/saxs_computation/uu/6uui/6uui.fit
pddf	/app/data/pr_computation/uu/6uui/6uui.pr.out
profile	/app/data/saxs_computation/uu/6uui/6uui.dat

Crystal structure of the heterocomplex between coil 2B domains of wild-type keratin 1 (KRT1) and keratin 10 (KRT10) containing mutation Cys401Ala

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

Keratin, type II cytoskeletal 1

State in the Current Structure

Other States of the Same Protein in the Database

Keratin, type I cytoskeletal 10

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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)