SAXSdb — 4jo7

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

Nucleoporin p54

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 453–491 Chain D； UniProt 453–491	Fragment：UNP residues 453-491	Nucleoporin p58/p45 × 2 （Q9BVL2）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；294 K；0.1 M MES, pH 6.5, 6.7% PEG20000, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 1.75 Å R-free 0.214
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain F； UniProt 453–491 Chain H； UniProt 453–491	Fragment：UNP residues 453-491	Nucleoporin p58/p45 × 2 （Q9BVL2）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；294 K；0.1 M MES, pH 6.5, 6.7% PEG20000, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 1.75 Å R-free 0.214

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 4JO7	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4JNU Crystal structure of the human Nup57CCS3* coiled-coil segment, space group P21 Deposited 2013-03-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 453–491（39 aa） Fragment：UNP residues 453-491 Chain B 453–491（39 aa） Fragment：UNP residues 453-491 Chain C 453–491（39 aa） Fragment：UNP residues 453-491 Chain D 453–491（39 aa） Fragment：UNP residues 453-491	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.3；294 K；0.1 M sodium acetate, pH 5.3, 1.9 M sodium formate, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 1.45 Å R-free 0.218
4JNV Crystal structure of the human Nup57CCS3* coiled-coil segment, space group C2 Deposited 2013-03-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 453–491（39 aa） Fragment：UNP residues 453-491 Chain B 453–491（39 aa） Fragment：UNP residues 453-491 Chain C 453–491（39 aa） Fragment：UNP residues 453-491 Chain D 453–491（39 aa） Fragment：UNP residues 453-491	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.3；294 K；0.1 M sodium acetate, pH 5.3, 1.9 M sodium formate, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 1.85 Å R-free 0.277
4JO9 Crystal structure of the human Nup49CCS2+3* Nup57CCS3* complex 1:2 stoichiometry Deposited 2013-03-18	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 453–491（39 aa） Fragment：UNP residues 453-491 Chain C 453–491（39 aa） Fragment：UNP residues 453-491	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 3.8；294 K；0.1 M sodium citrate, pH 3.8, 0.07 M calcium chloride, VAPOR DIFFUSION, temperature 294.0K	Resolution 2.50 Å R-free 0.294
5IJN Composite structure of the inner ring of the human nuclear pore complex (32 copies of Nup205) Deposited 2016-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 208 PDB declaration: 208-meric	Chain F 1–507（507 aa） Chain L 1–507（507 aa） Chain R 1–507（507 aa） Chain X 1–507（507 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 21.40 Å
5IJO Alternative composite structure of the inner ring of the human nuclear pore complex (16 copies of Nup188, 16 copies of Nup205) Deposited 2016-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 208 PDB declaration: 208-meric	Chain F 1–507（507 aa） Chain L 1–507（507 aa） Chain R 1–507（507 aa） Chain X 1–507（507 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 21.40 Å
7PER Model of the inner ring of the human nuclear pore complex Deposited 2021-08-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric	Chain F 1–507（507 aa） Chain L 1–507（507 aa） Chain R 1–507（507 aa） Chain X 1–507（507 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE；Cells were grown on holey carbon, Au-mesh supports. Grids were rinsed briefly with PBS and manually blotted before plunging into liquid ethane.	Resolution 35.00 Å
7R5J Human nuclear pore complex (dilated) Deposited 2022-02-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric	Chain H0 1–507（507 aa） Chain H1 1–507（507 aa） Chain H2 1–507（507 aa） Chain H3 1–507（507 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 50.00 Å
7R5K Human nuclear pore complex (constricted) Deposited 2022-02-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric	Chain H0 1–507（507 aa） Chain H1 1–507（507 aa） Chain H2 1–507（507 aa） Chain H3 1–507（507 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 12.00 Å

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NUP54_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain B； PDBConstruct 2–40； UniProt 453–491 Author chain D； PDBConstruct 2–40； UniProt 453–491 Author chain F； PDBConstruct 2–40； UniProt 453–491 Author chain H； PDBConstruct 2–40； UniProt 453–491

Nucleoporin p58/p45

Homo sapiens

UniProt Q9BVL2

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 341–428 Chain C； UniProt 341–428	Fragment：UNP residues 341-428 Non-standard monomer：Yes (specific site not provided by mmCIF)	Nucleoporin p54 × 2 （Q7Z3B4）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；294 K；0.1 M MES, pH 6.5, 6.7% PEG20000, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 1.75 Å R-free 0.214
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain E； UniProt 341–428 Chain G； UniProt 341–428	Fragment：UNP residues 341-428 Non-standard monomer：Yes (specific site not provided by mmCIF)	Nucleoporin p54 × 2 （Q7Z3B4）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；294 K；0.1 M MES, pH 6.5, 6.7% PEG20000, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 1.75 Å R-free 0.214

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 4JO7	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4JO9 Crystal structure of the human Nup49CCS2+3* Nup57CCS3* complex 1:2 stoichiometry Deposited 2013-03-18	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 B 341–426（86 aa） Fragment：UNP residues 341-426	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 3.8；294 K；0.1 M sodium citrate, pH 3.8, 0.07 M calcium chloride, VAPOR DIFFUSION, temperature 294.0K	Resolution 2.50 Å R-free 0.294
4JQ5 Crystal structure of the human Nup49CCS2+3* coiled-coil segment Deposited 2013-03-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 341–425（85 aa） Fragment：UNP residues 341-425 Chain B 341–425（85 aa） Fragment：UNP residues 341-425 Chain C 341–425（85 aa） Fragment：UNP residues 341-425 Chain D 341–425（85 aa） Fragment：UNP residues 341-425	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；294 K；10% glycerol, 28% dioxane, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 2.19 Å R-free 0.293
4JQ5 Crystal structure of the human Nup49CCS2+3* coiled-coil segment Deposited 2013-03-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 341–425（85 aa） Fragment：UNP residues 341-425 Chain F 341–425（85 aa） Fragment：UNP residues 341-425 Chain G 341–425（85 aa） Fragment：UNP residues 341-425 Chain H 341–425（85 aa） Fragment：UNP residues 341-425	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；294 K；10% glycerol, 28% dioxane, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 2.19 Å R-free 0.293
4JQ5 Crystal structure of the human Nup49CCS2+3* coiled-coil segment Deposited 2013-03-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain I 341–425（85 aa） Fragment：UNP residues 341-425 Chain J 341–425（85 aa） Fragment：UNP residues 341-425 Chain K 341–425（85 aa） Fragment：UNP residues 341-425 Chain L 341–425（85 aa） Fragment：UNP residues 341-425	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；294 K；10% glycerol, 28% dioxane, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 2.19 Å R-free 0.293
5IJN Composite structure of the inner ring of the human nuclear pore complex (32 copies of Nup205) Deposited 2016-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 208 PDB declaration: 208-meric	Chain G 1–599（599 aa） Chain M 1–599（599 aa） Chain S 1–599（599 aa） Chain Y 1–599（599 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 21.40 Å
5IJO Alternative composite structure of the inner ring of the human nuclear pore complex (16 copies of Nup188, 16 copies of Nup205) Deposited 2016-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 208 PDB declaration: 208-meric	Chain G 1–599（599 aa） Chain M 1–599（599 aa） Chain S 1–599（599 aa） Chain Y 1–599（599 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 21.40 Å
7PER Model of the inner ring of the human nuclear pore complex Deposited 2021-08-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric	Chain G 1–599（599 aa） Chain M 1–599（599 aa） Chain S 1–599（599 aa） Chain Y 1–599（599 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE；Cells were grown on holey carbon, Au-mesh supports. Grids were rinsed briefly with PBS and manually blotted before plunging into liquid ethane.	Resolution 35.00 Å
7R5J Human nuclear pore complex (dilated) Deposited 2022-02-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric	Chain I0 1–599（599 aa） Chain I1 1–599（599 aa） Chain I2 1–599（599 aa） Chain I3 1–599（599 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 50.00 Å
7R5K Human nuclear pore complex (constricted) Deposited 2022-02-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric	Chain I0 1–599（599 aa） Chain I1 1–599（599 aa） Chain I2 1–599（599 aa） Chain I3 1–599（599 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 12.00 Å

7 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NUPL1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 2–89； UniProt 341–428 Author chain C； PDBConstruct 2–89； UniProt 341–428 Author chain E； PDBConstruct 2–89； UniProt 341–428 Author chain G； PDBConstruct 2–89； UniProt 341–428

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	4jo7
Deposition date deposition_date	2013-03-17
Structure title title	Crystal structure of the human Nup49CCS2+3* Nup57CCS3* complex with 2:2 stoichiometry
Keywords keywords	Nucleocytoplasmic transport, TRANSPORT PROTEIN; TRANSPORT 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	27.13 Å
Radius of gyration Rg (electron density) rg_electron	26.40 Å
Forward intensity I(0) i0	55510500.00
Molecular weight molecular_weight	58723.0 kDa
Excluded volume excluded_volume	73618 Å³
Envelope volume envelope_volume	90526 Å³
Hydration-shell volume shell_volume	29411 Å³
Envelope diameter envelope_diameter	100.1 Å
Shell Rg shell_rg	32.52 Å
Envelope Rg envelope_rg	27.05 Å
Shape Rg shape_rg	26.41 Å
Total Rg total_rg	26.99 Å
Total atoms total_atoms	8227
Residues n_residues	481
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	96.9 Å
Rg (real space) rg_real	27.29 Å
Rg uncertainty (real space) rg_real_error	1.12 Å
I(0) (real space) i0_real	5.5510e+07
I(0) uncertainty (real space) i0_real_error	9.1420e+05
Rg (reciprocal space) rg_reciprocal	27.24 Å
I(0) (reciprocal space) i0_reciprocal	55510000.0000
Solution quality estimate total_estimate	0.8360
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	30.1 Å
Skewness Skewness skewness	0.559
Kurtosis Kurtosis kurtosis	-0.037
Angular range angular_range	— – 0.2900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	30500000.0000
Real-space data points n_real_points	59
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.670; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.898; Smooth: 0.957

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Nucleoporin p54
Molecular weight formula_weight	4729.4 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,H,D,F
Atom count atom_count	8763

SYYIDADLLREIKQHLKQQQEGLSHLISIIKDDLEDIKLV

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	Nucleoporin p58/p45
Molecular weight formula_weight	10522.4 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,G,A,C

SAPADYFRILVQQFEVQLQQYRQQIEELENHLATQANNSHITPQDLSMAMQKIYQTFVALAAQLQSIHENVKVLKEQYLGYRKMFLGDA

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 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	454

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7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id	4jo7A00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	1350 —

Domain ID domain_id	4jo7B00
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	170 —

Domain ID domain_id	4jo7C00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	1350 —

Domain ID domain_id	4jo7D00
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	170 —

Domain ID domain_id	4jo7E00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	1350 —

Domain ID domain_id	4jo7F00
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	170 —

Domain ID domain_id	4jo7G00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	1350 —

Domain ID domain_id	4jo7H00
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	170 —

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8. Citations (1)

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Unit-cell length a length_a	47.689 Å
Unit-cell length b length_b	47.658 Å
Unit-cell length c length_c	71.324 Å
Unit-cell angle α angle_alpha	88.87 °
Unit-cell angle β angle_beta	83.37 °
Unit-cell angle γ angle_gamma	81.42 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	1.752 Å
Low-resolution limit resolution_low	47.125 Å
R factor r_factor	0.1873
R_work r_work	0.1863
R_free r_free	0.2144

fit	/app/data/saxs_computation/jo/4jo7/4jo7.fit
pddf	/app/data/pr_computation/jo/4jo7/4jo7.pr.out
profile	/app/data/saxs_computation/jo/4jo7/4jo7.dat

Crystal structure of the human Nup49CCS2+3* Nup57CCS3* complex with 2:2 stoichiometry

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

Nucleoporin p54

State in the Current Structure

Other States of the Same Protein in the Database

Nucleoporin p58/p45

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 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)