SAXSdb — 3ij2

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

Beta-nerve growth factor

Mus musculus

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 129–351 Chain B； UniProt 129–351	Fragment：UNP RESIDUES 129-241	Nerve growth factor receptor (TNFR superfamily, member 16) × 2 （P07174）	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 3.75 Å R-free 0.274

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 3IJ2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BET NEW PROTEIN FOLD REVEALED BY A 2.3 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF NERVE GROWTH FACTOR Deposited 1993-04-08	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 131–237（107 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
1BTG CRYSTAL STRUCTURE OF BETA NERVE GROWTH FACTOR AT 2.5 A RESOLUTION IN C2 SPACE GROUP WITH ZN IONS BOUND Deposited 1995-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 130–239（110 aa） Chain B 130–239（110 aa） Chain C 130–239（110 aa）	Mutation：BIS-DES-OCTA (MISSING RESIDUES 1-8, PROTEOLYTICALLY CLEAVED) Mutation：BIS-DES-OCTA (MISSING RESIDUES 1-8, PROTEOLYTICALLY CLEAVED) Mutation：BIS-DES-OCTA (MISSING RESIDUES 1-8, PROTEOLYTICALLY CLEAVED)	ZN ZINC ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1BTG CRYSTAL STRUCTURE OF BETA NERVE GROWTH FACTOR AT 2.5 A RESOLUTION IN C2 SPACE GROUP WITH ZN IONS BOUND Deposited 1995-08-29	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 130–239（110 aa）	Mutation：BIS-DES-OCTA (MISSING RESIDUES 1-8, PROTEOLYTICALLY CLEAVED)	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1BTG CRYSTAL STRUCTURE OF BETA NERVE GROWTH FACTOR AT 2.5 A RESOLUTION IN C2 SPACE GROUP WITH ZN IONS BOUND Deposited 1995-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 130–239（110 aa） Chain C 130–239（110 aa）	Mutation：BIS-DES-OCTA (MISSING RESIDUES 1-8, PROTEOLYTICALLY CLEAVED) Mutation：BIS-DES-OCTA (MISSING RESIDUES 1-8, PROTEOLYTICALLY CLEAVED)	ZN ZINC ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1BTG CRYSTAL STRUCTURE OF BETA NERVE GROWTH FACTOR AT 2.5 A RESOLUTION IN C2 SPACE GROUP WITH ZN IONS BOUND Deposited 1995-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 130–239（110 aa） Chain C 130–239（110 aa）	Mutation：BIS-DES-OCTA (MISSING RESIDUES 1-8, PROTEOLYTICALLY CLEAVED) Mutation：BIS-DES-OCTA (MISSING RESIDUES 1-8, PROTEOLYTICALLY CLEAVED)	ZN ZINC ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1SGF CRYSTAL STRUCTURE OF 7S NGF: A COMPLEX OF NERVE GROWTH FACTOR WITH FOUR BINDING PROTEINS (SERINE PROTEINASES) Deposited 1997-08-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 122–239（118 aa） Chain Y 122–239（118 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.9；PROTEIN WAS CRYSTALLIZED FROM 20MG/ML PROTEIN SOLUTION IN 50MM SODIUM PHOSPHATE (PH6.8) MIXED WITH AN EQUAL VOLUME OF WELL SOLUTION (50MM SODIUM ACETATE PH4.5-5.1, 12-21% PEG 4000, 10 MICROMOLAR ZNSO4) (MCDONALD AND BLUNDELL, 1991, JMB, 219, 595-601)., pH 4.9	Resolution 3.15 Å R-free 0.282
4EAX Mouse NGF in complex with Lyso-PS Deposited 2012-03-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 122–241（120 aa） Chain B 122–241（120 aa）	Not recorded	S12 O-[(S)-hydroxy{[(2S)-2-hydroxy-3-(octadec-9-enoyloxy)propyl]oxy}phosphoryl]-L-serine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；289 K；0.1M Imidazole, 1.0M Sodium Acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 2.30 Å R-free 0.259
4EAX Mouse NGF in complex with Lyso-PS Deposited 2012-03-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 122–241（120 aa） Chain D 122–241（120 aa）	Not recorded	S12 O-[(S)-hydroxy{[(2S)-2-hydroxy-3-(octadec-9-enoyloxy)propyl]oxy}phosphoryl]-L-serine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；289 K；0.1M Imidazole, 1.0M Sodium Acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 2.30 Å R-free 0.259
4XPJ Crystal structure of Nerve growth factor in complex with lysophosphatidylinositol Deposited 2015-01-17	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 122–241（120 aa） Chain B 122–241（120 aa）	Not recorded	LPY (2R)-2-hydroxy-3-{[(S)-hydroxy{[(1S,2R,3R,4S,5S,6R)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}propyl tridecanoate × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；289 K；0.1 M imidazole, 1.0 M Na acetate	Resolution 2.60 Å R-free 0.266
5LSD Recombinant mouse Nerve Growth Factor Deposited 2016-08-25	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 122–239（118 aa） Chain B 122–239（118 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；303 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR measurement conditions pH 7；308 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 0.1 mM [U-99% 13C; U-99% 15N] Nerve Growth Factor, 50 mM sodium phosphate, 1 mM EDTA, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
6FFY Structure of the mouse SorCS2-NGF complex Deposited 2018-01-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 122–238（117 aa） Chain C 122–238（117 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.6；291 K；0.225 M MES/bis-tris pH 6.6 and 6.6 % w/v PEG 6000	Resolution 3.90 Å R-free 0.305

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

View Construct and Data Evidence

UniProt name	NGF_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–223； UniProt 129–351 Author chain B； PDBConstruct 1–223； UniProt 129–351

Nerve growth factor receptor (TNFR superfamily, member 16)

Rattus norvegicus

UniProt P07174

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 X； UniProt 33–193 Chain Y； UniProt 33–193	Fragment：UNP RESIDUES 30-190	Beta-nerve growth factor × 2 （P01139）	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 3.75 Å R-free 0.274

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 3IJ2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1NGR DEATH DOMAIN OF P75 LOW AFFINITY NEUROTROPHIN RECEPTOR, RESIDUES 334-418, NMR, 20 STRUCTURES Deposited 1997-01-28	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 334–418（85 aa） Fragment：DEATH DOMAIN, RESIDUES 281 - 425	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；301 K	Resolution not provided
1SG1 Crystal Structure of the Receptor-Ligand Complex between Nerve Growth Factor and the Common Neurotrophin Receptor p75 Deposited 2004-02-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain X 30–190（161 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.3；295 K；PEG 1000, isoproponal, sodium chloride, citrate, pH 6.3, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.40 Å R-free 0.269
2MIC NMR structure of p75 transmembrane domain in DPC micelles Deposited 2013-12-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 245–284（40 aa） Fragment：UNP residues 245-284 Chain B 245–284（40 aa） Fragment：UNP residues 245-284	Mutation：C36S (chain A), C136S (chain B) Mutation：C36S (chain A), C136S (chain B)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.9；318 K；Pressure ambient NMR sample composition 1.9 mM [U-100% 13C; U-100% 15N] p75-TM-wt, 95 mM [U-98% 2H] DPC, 20 mM sodium phosphate, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2MJO NMR structure of p75 transmembrane domain C257A mutant in DPC micelles Deposited 2014-01-15	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 245–284（40 aa） Fragment：UNP residues 245-284 Chain B 245–284（40 aa） Fragment：UNP residues 245-284	Mutation：C14A, C36S chain A, C114A, C136S chain B Mutation：C14A, C36S chain A, C114A, C136S chain B	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.9；318 K；Pressure ambient NMR sample composition 1.5 mM [U-100% 13C; U-100% 15N] p75-TM-C257A, 30 mM [U-98% 2H] DPC, 20 mM sodium phosphate, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
3BUK Crystal Structure of the Neurotrophin-3 and p75NTR Symmetrical Complex Deposited 2008-01-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 29–189（161 aa） Fragment：ectodomain Chain D 29–189（161 aa） Fragment：ectodomain	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5；290 K；0.9M Lithium Sulfate, 0.05M Na Citrate, 0.7M Ammonium Sulfate, pH 5.0, EVAPORATION, temperature 290K	Resolution 2.60 Å R-free 0.288
4F42 Neurotrophin p75NTR intracellular domain Deposited 2012-05-09	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 334–418（85 aa） Fragment：death domain, UNP RESIDUES 334-418	Not recorded	MNB 5-MERCAPTO-2-NITRO-BENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；0.1M Bis-Tris propane pH 7.0, 1.2M sodium citrate tribasic dehydrate, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.38 Å R-free 0.260
4F44 Neurotrophin p75NTR intracellular domain Deposited 2012-05-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 334–418（85 aa） Fragment：death domain Chain B 334–418（85 aa） Fragment：death domain	Not recorded	MNB 5-MERCAPTO-2-NITRO-BENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；0.1M Bis-Tris propane, 1.4M sodium malonate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.40 Å R-free 0.280

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

View Construct and Data Evidence

UniProt name	P07174_RAT
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain X； PDBConstruct 4–164； UniProt 33–193 Author chain Y； PDBConstruct 4–164； UniProt 33–193

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	3ij2
Deposition date deposition_date	2009-08-03
Structure title title	Ligand-receptor structure
Keywords keywords	;Receptor and ligand, Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Growth factor, Phosphoprotein, Secreted, HORMONE-PROTEIN BINDING COMPLEX ;; HORMONE/PROTEIN BINDING
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	30.09 Å
Radius of gyration Rg (electron density) rg_electron	29.27 Å
Forward intensity I(0) i0	68547400.00
Molecular weight molecular_weight	59040.0 kDa
Excluded volume excluded_volume	71263 Å³
Envelope volume envelope_volume	97911 Å³
Hydration-shell volume shell_volume	29456 Å³
Envelope diameter envelope_diameter	106.9 Å
Shell Rg shell_rg	34.40 Å
Envelope Rg envelope_rg	29.64 Å
Shape Rg shape_rg	29.25 Å
Total Rg total_rg	29.78 Å
Total atoms total_atoms	4092
Residues n_residues	542
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	103.2 Å
Rg (real space) rg_real	30.18 Å
Rg uncertainty (real space) rg_real_error	1.14 Å
I(0) (real space) i0_real	6.8550e+07
I(0) uncertainty (real space) i0_real_error	1.1100e+06
Rg (reciprocal space) rg_reciprocal	30.15 Å
I(0) (reciprocal space) i0_reciprocal	68550000.0000
Solution quality estimate total_estimate	0.8787
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	31.1 Å
Skewness Skewness skewness	0.409
Kurtosis Kurtosis kurtosis	-0.254
Angular range angular_range	— – 0.2650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3710000.0000
Real-space data points n_real_points	54
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.913

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Beta-nerve growth factor
Molecular weight formula_weight	25450.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4092

EPYTDSNVPEGDSVPEAHWTKLQHSLDTALAAARSAPTAPIAARVTGQTRNITVDPRLFKAARLHSPRVLFSTQPPPTSSDTLDLDFQAHGTIPFNRTHRSAASSTHPVFHMGEFSVCDSVSVWVGDKTTATDIKGKEVTVLAEVNINNSVFRQYFFETKCRASNPVESGCRGIDSKHWNSYCTTTHTFVKALTTDEKQAAWRFIRIDTACVCVLSRKATAAGHHHHHHH

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Trichoplusia ni

Entity 2 Entity 2 polymer

Description description	Nerve growth factor receptor (TNFR superfamily, member 16)
Molecular weight formula_weight	18482.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	X,Y

ADPKETCSTGLYTHSGECCKACNLGEGVAQPCGADQTVCEPCLDSVTFSDVVSATEPCKPCTECLGLQSMSAPCVEADDAVCRCAYGYYQDEETGHCEACSVCEVGSGLVFSCQDKQNTVCEECPEGTYSDEANHVDPCLPCTVCEDTERQLRECTPWADAECEHHHHHHH

来源 Source

来源生物 organism	Rattus norvegicus
通用名 common_name	rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Trichoplusia ni

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7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id	3ij2A00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily	10 — Cystine-knot cytokines

Domain ID domain_id	3ij2B00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily	10 — Cystine-knot cytokines

Domain ID domain_id	3ij2X01
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	50 — Tumor Necrosis Factor Receptor, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Tumor Necrosis Factor Receptor, subunit A, domain 2

Domain ID domain_id	3ij2X02
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	50 — Tumor Necrosis Factor Receptor, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Tumor Necrosis Factor Receptor, subunit A, domain 2

Domain ID domain_id	3ij2Y01
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	50 — Tumor Necrosis Factor Receptor, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Tumor Necrosis Factor Receptor, subunit A, domain 2

Domain ID domain_id	3ij2Y02
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	50 — Tumor Necrosis Factor Receptor, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Tumor Necrosis Factor Receptor, subunit A, domain 2

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8. Citations (1)

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Unit-cell length a length_a	145.406 Å
Unit-cell length b length_b	145.406 Å
Unit-cell length c length_c	114.252 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 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	3.750 Å
Low-resolution limit resolution_low	47.595 Å
R factor r_factor	0.2565
R_work r_work	0.2556
R_free r_free	0.2739

fit	/app/data/saxs_computation/ij/3ij2/3ij2.fit
pddf	/app/data/pr_computation/ij/3ij2/3ij2.pr.out
profile	/app/data/saxs_computation/ij/3ij2/3ij2.dat

Ligand-receptor structure

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

Beta-nerve growth factor

State in the Current Structure

Other States of the Same Protein in the Database

Nerve growth factor receptor (TNFR superfamily, member 16)

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)