SAXSdb — 3wut

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

Centrosomal protein of 55 kDa

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 160–217 Chain B； UniProt 160–217	Fragment：UNP residues 160-217	Inactive serine/threonine-protein kinase TEX14 × 1 （Q8IWB6） GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；295 K；1M ammonium phosphate dibasic, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.30 Å R-free 0.259
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 160–217 Chain E； UniProt 160–217	Fragment：UNP residues 160-217	Inactive serine/threonine-protein kinase TEX14 × 1 （Q8IWB6） GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；295 K；1M ammonium phosphate dibasic, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.30 Å R-free 0.259
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain G； UniProt 160–217 Chain H； UniProt 160–217	Fragment：UNP residues 160-217	Inactive serine/threonine-protein kinase TEX14 × 1 （Q8IWB6）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；295 K；1M ammonium phosphate dibasic, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.30 Å R-free 0.259
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain J； UniProt 160–217 Chain K； UniProt 160–217	Fragment：UNP residues 160-217	Inactive serine/threonine-protein kinase TEX14 × 1 （Q8IWB6）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；295 K；1M ammonium phosphate dibasic, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.30 Å R-free 0.259

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 3WUT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3E1R Midbody targeting of the ESCRT machinery by a non-canonical coiled-coil in CEP55 Deposited 2008-08-04	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 160–217（58 aa） Fragment：UNP residues 160-217 Chain B 160–217（58 aa） Fragment：UNP residues 160-217	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；294 K；100 mM MES, 22% PEG 6000, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.00 Å R-free 0.248
3WUU Structure basis of inactivating cell abscission with chimera peptide 1 Deposited 2014-05-05	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 160–217（58 aa） Fragment：UNP residues 160-217 Chain B 160–217（58 aa） Fragment：UNP residues 160-217	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；295 K；20%(w/v) polyacrylic acid 5100, 0.2M magnesium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.90 Å R-free 0.260
3WUU Structure basis of inactivating cell abscission with chimera peptide 1 Deposited 2014-05-05	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 160–217（58 aa） Fragment：UNP residues 160-217 Chain E 160–217（58 aa） Fragment：UNP residues 160-217	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；295 K；20%(w/v) polyacrylic acid 5100, 0.2M magnesium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.90 Å R-free 0.260
3WUU Structure basis of inactivating cell abscission with chimera peptide 1 Deposited 2014-05-05	Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 160–217（58 aa） Fragment：UNP residues 160-217 Chain H 160–217（58 aa） Fragment：UNP residues 160-217	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；295 K；20%(w/v) polyacrylic acid 5100, 0.2M magnesium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.90 Å R-free 0.260
3WUU Structure basis of inactivating cell abscission with chimera peptide 1 Deposited 2014-05-05	Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain J 160–217（58 aa） Fragment：UNP residues 160-217 Chain K 160–217（58 aa） Fragment：UNP residues 160-217	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；295 K；20%(w/v) polyacrylic acid 5100, 0.2M magnesium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.90 Å R-free 0.260
3WUV Structure basis of inactivating cell abscission with chimera peptide 2 Deposited 2014-05-05	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 160–217（58 aa） Fragment：UNP residues 160-217 Chain B 160–217（58 aa） Fragment：UNP residues 160-217	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；295 K；0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.79 Å R-free 0.227
3WUV Structure basis of inactivating cell abscission with chimera peptide 2 Deposited 2014-05-05	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 160–217（58 aa） Fragment：UNP residues 160-217 Chain E 160–217（58 aa） Fragment：UNP residues 160-217	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；295 K；0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.79 Å R-free 0.227
3WUV Structure basis of inactivating cell abscission with chimera peptide 2 Deposited 2014-05-05	Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 160–217（58 aa） Fragment：UNP residues 160-217 Chain H 160–217（58 aa） Fragment：UNP residues 160-217	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；295 K；0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.79 Å R-free 0.227
3WUV Structure basis of inactivating cell abscission with chimera peptide 2 Deposited 2014-05-05	Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain J 160–217（58 aa） Fragment：UNP residues 160-217 Chain K 160–217（58 aa） Fragment：UNP residues 160-217	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；295 K；0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.79 Å R-free 0.227
3WUV Structure basis of inactivating cell abscission with chimera peptide 2 Deposited 2014-05-05	Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain M 160–217（58 aa） Fragment：UNP residues 160-217 Chain N 160–217（58 aa） Fragment：UNP residues 160-217	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；295 K；0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.79 Å R-free 0.227
3WUV Structure basis of inactivating cell abscission with chimera peptide 2 Deposited 2014-05-05	Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain P 160–217（58 aa） Fragment：UNP residues 160-217 Chain Q 160–217（58 aa） Fragment：UNP residues 160-217	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；295 K；0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.79 Å R-free 0.227

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

View Construct and Data Evidence

UniProt name	CEP55_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–63； UniProt 160–217 Author chain B； PDBConstruct 6–63； UniProt 160–217 Author chain D； PDBConstruct 6–63； UniProt 160–217 Author chain E； PDBConstruct 6–63； UniProt 160–217 Author chain G； PDBConstruct 6–63； UniProt 160–217 Author chain H； PDBConstruct 6–63； UniProt 160–217 Author chain J； PDBConstruct 6–63； UniProt 160–217 Author chain K； PDBConstruct 6–63； UniProt 160–217

Inactive serine/threonine-protein kinase TEX14

OrganismNot specified

UniProt Q8IWB6

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain C； UniProt 792–804	Fragment：UNP residues 792-804	Centrosomal protein of 55 kDa × 2 （Q53EZ4） GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；295 K；1M ammonium phosphate dibasic, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.30 Å R-free 0.259
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain F； UniProt 792–804	Fragment：UNP residues 792-804	Centrosomal protein of 55 kDa × 2 （Q53EZ4） GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；295 K；1M ammonium phosphate dibasic, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.30 Å R-free 0.259
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain I； UniProt 792–804	Fragment：UNP residues 792-804	Centrosomal protein of 55 kDa × 2 （Q53EZ4）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；295 K；1M ammonium phosphate dibasic, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.30 Å R-free 0.259
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain L； UniProt 792–804	Fragment：UNP residues 792-804	Centrosomal protein of 55 kDa × 2 （Q53EZ4）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；295 K；1M ammonium phosphate dibasic, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.30 Å R-free 0.259

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 3WUT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3WUU Structure basis of inactivating cell abscission with chimera peptide 1 Deposited 2014-05-05	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 791–804（14 aa）	Mutation：P791D/I802P/P803G/P804Y	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；295 K；20%(w/v) polyacrylic acid 5100, 0.2M magnesium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.90 Å R-free 0.260
3WUU Structure basis of inactivating cell abscission with chimera peptide 1 Deposited 2014-05-05	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 791–804（14 aa）	Mutation：P791D/I802P/P803G/P804Y	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；295 K；20%(w/v) polyacrylic acid 5100, 0.2M magnesium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.90 Å R-free 0.260
3WUU Structure basis of inactivating cell abscission with chimera peptide 1 Deposited 2014-05-05	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain L 791–804（14 aa）	Mutation：P791D/I802P/P803G/P804Y	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；295 K；20%(w/v) polyacrylic acid 5100, 0.2M magnesium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.90 Å R-free 0.260
3WUU Structure basis of inactivating cell abscission with chimera peptide 1 Deposited 2014-05-05	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 791–804（14 aa）	Mutation：P791D/I802P/P803G/P804Y	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；295 K；20%(w/v) polyacrylic acid 5100, 0.2M magnesium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.90 Å R-free 0.260

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

View Construct and Data Evidence

UniProt name	TEX14_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 2–14； UniProt 792–804 Author chain F； PDBConstruct 2–14； UniProt 792–804 Author chain I； PDBConstruct 2–14； UniProt 792–804 Author chain L； PDBConstruct 2–14； UniProt 792–804

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	3wut
Deposition date deposition_date	2014-05-05
Structure title title	Structure basis of inactivating cell abscission
Keywords keywords	Coiled-coil, CELL CYCLE; CELL CYCLE
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	30.39 Å
Radius of gyration Rg (electron density) rg_electron	29.54 Å
Forward intensity I(0) i0	42341000.00
Molecular weight molecular_weight	52696.0 kDa
Excluded volume excluded_volume	66966 Å³
Envelope volume envelope_volume	91869 Å³
Hydration-shell volume shell_volume	27356 Å³
Envelope diameter envelope_diameter	104.0 Å
Shell Rg shell_rg	34.45 Å
Envelope Rg envelope_rg	30.26 Å
Shape Rg shape_rg	29.47 Å
Total Rg total_rg	30.32 Å
Total atoms total_atoms	3718
Residues n_residues	447
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	98.8 Å
Rg (real space) rg_real	30.35 Å
Rg uncertainty (real space) rg_real_error	0.89 Å
I(0) (real space) i0_real	4.2340e+07
I(0) uncertainty (real space) i0_real_error	6.7950e+05
Rg (reciprocal space) rg_reciprocal	30.37 Å
I(0) (reciprocal space) i0_reciprocal	42340000.0000
Solution quality estimate total_estimate	0.9049
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	39.9 Å
Skewness Skewness skewness	0.183
Kurtosis Kurtosis kurtosis	-0.523
Angular range angular_range	— – 0.2600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2465000.0000
Real-space data points n_real_points	53
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.946; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.942

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Centrosomal protein of 55 kDa
Molecular weight formula_weight	7243.2 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,D,E,G,H,J,K
Atom count atom_count	3906

GAMGSFNSSINNIHEMEIQLKDALEKNQQWLVYDQQREVYVKGLLAKIFELEKKTETAAHSLP

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

Entity 2 Entity 2 polymer

Description description	Inactive serine/threonine-protein kinase TEX14
Molecular weight formula_weight	1452.7 kDa
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

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

DLAVGPPSLNYIPP

Entity 3 Entity 3 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	188

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7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id	3wutA00
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	1180 — Geminin coiled-coil domain

Domain ID domain_id	3wutB00
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	1180 — Geminin coiled-coil domain

Domain ID domain_id	3wutD00
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	1180 — Geminin coiled-coil domain

Domain ID domain_id	3wutE00
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	1180 — Geminin coiled-coil domain

Domain ID domain_id	3wutG00
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	1180 — Geminin coiled-coil domain

Domain ID domain_id	3wutH00
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	1180 — Geminin coiled-coil domain

Domain ID domain_id	3wutJ00
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	1180 — Geminin coiled-coil domain

Domain ID domain_id	3wutK00
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	1180 — Geminin coiled-coil domain

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8. Citations (1)

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Unit-cell length a length_a	53.913 Å
Unit-cell length b length_b	102.622 Å
Unit-cell length c length_c	132.535 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	32

Space group space_group	P 2 21 21
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.301 Å
Low-resolution limit resolution_low	28.884 Å
R factor r_factor	0.2221
R_work r_work	0.2202
R_free r_free	0.2588

fit	/app/data/saxs_computation/wu/3wut/3wut.fit
pddf	/app/data/pr_computation/wu/3wut/3wut.pr.out
profile	/app/data/saxs_computation/wu/3wut/3wut.dat

Structure basis of inactivating cell abscission

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

Centrosomal protein of 55 kDa

State in the Current Structure

Other States of the Same Protein in the Database

Inactive serine/threonine-protein kinase TEX14

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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)