SAXSdb — 2hfg

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

CB3s Fab light chain (kappa)

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 L； UniProt 23–236	Not recorded	CB3s Fab heavy chain × 1 （Q6N093） Tumor necrosis factor receptor superfamily member 13C × 1 （Q96RJ3）	X-RAY DIFFRACTION X-ray crystallization conditions：Drops contained 2.1 microliters protein solution (pH 6.5) and 2.9 microliters of (0.1M citric acid pH 3.0, 24% PEG 3350, and 0.1 M Praseodymium (III) acetate) over a reservoir of 24% PEG 3350. pH of final drop ~4.5.	Resolution 2.61 Å R-free 0.252

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 2HFG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2AJ3 Crystal Structure of a Cross-Reactive HIV-1 Neutralizing CD4-Binding Site Antibody Fab m18 Deposited 2005-08-01	Different construct 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 25–236（212 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.5；292 K；100 mM CHES, 20% (w/v) PEG-8000, pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.03 Å R-free 0.269
2AJ3 Crystal Structure of a Cross-Reactive HIV-1 Neutralizing CD4-Binding Site Antibody Fab m18 Deposited 2005-08-01	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 25–236（212 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.5；292 K；100 mM CHES, 20% (w/v) PEG-8000, pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.03 Å R-free 0.269
2AJ3 Crystal Structure of a Cross-Reactive HIV-1 Neutralizing CD4-Binding Site Antibody Fab m18 Deposited 2005-08-01	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 25–236（212 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.5；292 K；100 mM CHES, 20% (w/v) PEG-8000, pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.03 Å R-free 0.269

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

View Construct and Data Evidence

UniProt name	Q6PIH7_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain L； PDBConstruct 1–214； UniProt 23–236

CB3s Fab heavy chain

Homo sapiens

UniProt Q6N093

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 H； UniProt 1–194	Not recorded	CB3s Fab light chain (kappa) × 1 （Q6PIH7） Tumor necrosis factor receptor superfamily member 13C × 1 （Q96RJ3）	X-RAY DIFFRACTION X-ray crystallization conditions：Drops contained 2.1 microliters protein solution (pH 6.5) and 2.9 microliters of (0.1M citric acid pH 3.0, 24% PEG 3350, and 0.1 M Praseodymium (III) acetate) over a reservoir of 24% PEG 3350. pH of final drop ~4.5.	Resolution 2.61 Å R-free 0.252

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 2HFG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9N5P CRYSTAL STRUCTURE OF HUMAN IGG2 FC FRAGMENT-FC-GAMMA RECEPTOR IIA COMPLEX H131 VARIANT Deposited 2025-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 195–417（223 aa） Chain B 195–417（223 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；0.1 M HEPES pH 7.5, 25% PEG 2000 MME	Resolution 2.01 Å R-free 0.232

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

View Construct and Data Evidence

UniProt name	Q6N093_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain H； PDBConstruct 29–228； UniProt 1–194

Tumor necrosis factor receptor superfamily member 13C

Homo sapiens

UniProt Q96RJ3

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 R； UniProt 7–54	Fragment：cysteine rich domain (residues 7-54) Mutation：V20N, L27P	CB3s Fab light chain (kappa) × 1 （Q6PIH7） CB3s Fab heavy chain × 1 （Q6N093）	X-RAY DIFFRACTION X-ray crystallization conditions：Drops contained 2.1 microliters protein solution (pH 6.5) and 2.9 microliters of (0.1M citric acid pH 3.0, 24% PEG 3350, and 0.1 M Praseodymium (III) acetate) over a reservoir of 24% PEG 3350. pH of final drop ~4.5.	Resolution 2.61 Å R-free 0.252

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 2HFG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1MPV Structure of bhpBR3, the BAFF-binding loop of BR3 embedded in a beta-hairpin peptide Deposited 2002-09-12	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 26–31（6 aa） Fragment：BR3 loop (residues 26-31)	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.5；293 K；Ionic strength (raw mmCIF value) no added salt；Pressure ambient NMR sample composition 2.9 mM bhpBR3 peptide \| 92% H2O, 8% D2O, 0.1 mM DSS, pH 4.5 NMR sample composition 2.9 mM bhpBR3 peptide \| 100% D2O, 0.1 mM DSS, pH 4.5	Resolution not provided
1OQE Crystal structure of sTALL-1 with BAFF-R Deposited 2003-03-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 108 PDB declaration: 108-meric	Chain K 16–46（31 aa） Fragment：extracellular domain Chain L 16–46（31 aa） Fragment：extracellular domain Chain M 16–46（31 aa） Fragment：extracellular domain Chain N 16–46（31 aa） Fragment：extracellular domain Chain O 16–46（31 aa） Fragment：extracellular domain Chain P 16–46（31 aa） Fragment：extracellular domain Chain Q 16–46（31 aa） Fragment：extracellular domain Chain R 16–46（31 aa） Fragment：extracellular domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；dioxane, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 100K	Resolution 2.50 Å R-free 0.259
1OSX Solution Structure of the Extracellular Domain of BLyS Receptor 3 (BR3) Deposited 2003-03-20	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 1–61（61 aa） Fragment：extracellular domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；293 K；Ionic strength (raw mmCIF value) 50 mM NaCl, 25 mM Na2PO4；Pressure ambient NMR sample composition 1.5 mM BR3 U-15N,25 mM Na2PO4, 50 mM NaCl, 0.1 mM NaN3, 0.1 mM DSS-d10 \| 92%H2O/8%D2O NMR sample composition 1.5 mM BR3 U-15N,13C,25 mM Na2PO4, 50 mM NaCl, 0.1 mM NaN3, 0.1 mM DSS-d10 \| 92%H2O/8%D2O NMR sample composition 1.5 mM BR3 U-15N,13C,25 mM Na2PO4, 50 mM NaCl, 0.1 mM NaN3, 0.1 mM DSS-d10 \| 100% D2O	Resolution not provided
4V46 Crystal structure of the BAFF-BAFF-R complex Deposited 2003-03-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 120 PDB declaration: 120-meric	Chain B0 1–63（63 aa） Fragment：residues 1-63 Chain B1 1–63（63 aa） Fragment：residues 1-63 Chain B2 1–63（63 aa） Fragment：residues 1-63 Chain B3 1–63（63 aa） Fragment：residues 1-63 Chain B4 1–63（63 aa） Fragment：residues 1-63 Chain B5 1–63（63 aa） Fragment：residues 1-63 Chain B6 1–63（63 aa） Fragment：residues 1-63 Chain B7 1–63（63 aa） Fragment：residues 1-63 Chain B8 1–63（63 aa） Fragment：residues 1-63 Chain B9 1–63（63 aa） Fragment：residues 1-63 Chain BA 1–63（63 aa） Fragment：residues 1-63 Chain BB 1–63（63 aa） Fragment：residues 1-63 Chain BC 1–63（63 aa） Fragment：residues 1-63 Chain BD 1–63（63 aa） Fragment：residues 1-63 Chain BE 1–63（63 aa） Fragment：residues 1-63 Chain BF 1–63（63 aa） Fragment：residues 1-63 Chain BG 1–63（63 aa） Fragment：residues 1-63 Chain BH 1–63（63 aa） Fragment：residues 1-63 Chain BI 1–63（63 aa） Fragment：residues 1-63 Chain BJ 1–63（63 aa） Fragment：residues 1-63 Chain BK 1–63（63 aa） Fragment：residues 1-63 Chain BL 1–63（63 aa） Fragment：residues 1-63 Chain BM 1–63（63 aa） Fragment：residues 1-63 Chain BN 1–63（63 aa） Fragment：residues 1-63 Chain BO 1–63（63 aa） Fragment：residues 1-63 Chain BP 1–63（63 aa） Fragment：residues 1-63 Chain BQ 1–63（63 aa） Fragment：residues 1-63 Chain BR 1–63（63 aa） Fragment：residues 1-63 Chain BS 1–63（63 aa） Fragment：residues 1-63 Chain BT 1–63（63 aa） Fragment：residues 1-63 Chain BU 1–63（63 aa） Fragment：residues 1-63 Chain BV 1–63（63 aa） Fragment：residues 1-63 Chain BW 1–63（63 aa） Fragment：residues 1-63 Chain BX 1–63（63 aa） Fragment：residues 1-63 Chain BY 1–63（63 aa） Fragment：residues 1-63 Chain BZ 1–63（63 aa） Fragment：residues 1-63 Chain Ba 1–63（63 aa） Fragment：residues 1-63 Chain Bb 1–63（63 aa） Fragment：residues 1-63 Chain Bc 1–63（63 aa） Fragment：residues 1-63 Chain Bd 1–63（63 aa） Fragment：residues 1-63 Chain Be 1–63（63 aa） Fragment：residues 1-63 Chain Bf 1–63（63 aa） Fragment：residues 1-63 Chain Bg 1–63（63 aa） Fragment：residues 1-63 Chain Bh 1–63（63 aa） Fragment：residues 1-63 Chain Bi 1–63（63 aa） Fragment：residues 1-63 Chain Bj 1–63（63 aa） Fragment：residues 1-63 Chain Bk 1–63（63 aa） Fragment：residues 1-63 Chain Bl 1–63（63 aa） Fragment：residues 1-63 Chain Bm 1–63（63 aa） Fragment：residues 1-63 Chain Bn 1–63（63 aa） Fragment：residues 1-63 Chain Bo 1–63（63 aa） Fragment：residues 1-63 Chain Bp 1–63（63 aa） Fragment：residues 1-63 Chain Bq 1–63（63 aa） Fragment：residues 1-63 Chain Br 1–63（63 aa） Fragment：residues 1-63 Chain Bs 1–63（63 aa） Fragment：residues 1-63 Chain Bt 1–63（63 aa） Fragment：residues 1-63 Chain Bu 1–63（63 aa） Fragment：residues 1-63 Chain Bv 1–63（63 aa） Fragment：residues 1-63 Chain Bw 1–63（63 aa） Fragment：residues 1-63 Chain Bx 1–63（63 aa） Fragment：residues 1-63	Not recorded	MG MAGNESIUM ION × 40	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；sodium formate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 3.30 Å R-free 0.226
8ZUJ Pentagonal cluster of BAFF-BAFFR ectodomain complex Deposited 2024-06-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain A 2–78（77 aa） Chain B 2–78（77 aa） Chain C 2–78（77 aa） Chain G 2–78（77 aa） Chain H 2–78（77 aa） Chain I 2–78（77 aa） Chain M 2–78（77 aa） Chain N 2–78（77 aa） Chain O 2–78（77 aa） Chain S 2–78（77 aa） Chain T 2–78（77 aa） Chain U 2–78（77 aa） Chain Y 2–78（77 aa） Chain Z 2–78（77 aa） Chain a 2–78（77 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.58 Å
8ZUK Cluster structure of the BAFF-BAFFR-TRAF3 complex Deposited 2024-06-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 42 PDB declaration: 42-meric	Chain D 1–184（184 aa） Chain E 1–184（184 aa） Chain F 1–184（184 aa） Chain J 1–184（184 aa） Chain K 1–184（184 aa） Chain L 1–184（184 aa） Chain P 1–184（184 aa） Chain Q 1–184（184 aa） Chain R 1–184（184 aa） Chain V 1–184（184 aa） Chain W 1–184（184 aa） Chain X 1–184（184 aa） Chain b 1–184（184 aa） Chain c 1–184（184 aa） Chain d 1–184（184 aa） Chain h 1–184（184 aa） Chain i 1–184（184 aa） Chain j 1–184（184 aa） Chain n 1–184（184 aa） Chain o 1–184（184 aa） Chain p 1–184（184 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.83 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TR13C_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain R； PDBConstruct 4–51； UniProt 7–54

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	2hfg
Deposition date deposition_date	2006-06-23
Structure title title	Crystal structure of hBR3 bound to CB3s-Fab
Keywords keywords	fab fragment, TNFRSF, antibody-receptor complex, CRD, IMMUNE SYSTEM; IMMUNE SYSTEM
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	25.91 Å
Radius of gyration Rg (electron density) rg_electron	25.10 Å
Forward intensity I(0) i0	41109200.00
Molecular weight molecular_weight	49044.0 kDa
Excluded volume excluded_volume	61093 Å³
Envelope volume envelope_volume	76368 Å³
Hydration-shell volume shell_volume	25792 Å³
Envelope diameter envelope_diameter	90.0 Å
Shell Rg shell_rg	31.91 Å
Envelope Rg envelope_rg	25.02 Å
Shape Rg shape_rg	25.07 Å
Total Rg total_rg	25.96 Å
Total atoms total_atoms	3448
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	87.1 Å
Rg (real space) rg_real	25.94 Å
Rg uncertainty (real space) rg_real_error	0.76 Å
I(0) (real space) i0_real	4.1110e+07
I(0) uncertainty (real space) i0_real_error	6.5700e+05
Rg (reciprocal space) rg_reciprocal	25.93 Å
I(0) (reciprocal space) i0_reciprocal	41110000.0000
Solution quality estimate total_estimate	0.8896
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	28.5 Å
Skewness Skewness skewness	0.358
Kurtosis Kurtosis kurtosis	-0.370
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7326000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.982

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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	CB3s Fab light chain (kappa)
Molecular weight formula_weight	23250.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L
Atom count atom_count	3475

DIQMTQSPSSLSASVGDRVTITCRASQDVSTAVAWYQQKPGKAPKLLIYSASFLYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSQISPPTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

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	CB3s Fab heavy chain
Molecular weight formula_weight	24414.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

EVQLVESGGGLVQPGGSLRLSCAASGFTISSSSIHWVRQAPGKGLEWVAWVLPSVGFTDYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARRVCYNRLGVCAGGMDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTH

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 polymer

Description description	Tumor necrosis factor receptor superfamily member 13C
Molecular weight formula_weight	5323.1 kDa
Mutation mutation	V20N, L27P
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	R

GSYSLRGRDAPAPTPCNPAECFDPLVRHCVACGLLRTPRPKPAGASSPAPR

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 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	27

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7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (5 domains)

Domain ID domain_id	d2hfgh1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

Domain ID domain_id	d2hfgh2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.2 — C1 set domains (antibody constant domain-like)

Domain ID domain_id	d2hfgl1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

Domain ID domain_id	d2hfgl2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.2 — C1 set domains (antibody constant domain-like)

Domain ID domain_id	d2hfgr_
Class class	g — Small proteins
Fold Fold fold	g.24 — TNF receptor-like
Superfamily Superfamily superfamily	g.24.1 — TNF receptor-like
Family Family family	g.24.1.2 — BAFF receptor-like

CATH v4.4 (4 domains)

Domain ID domain_id	2hfgH01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	2hfgH02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	2hfgL01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	2hfgL02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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8. Citations (1)

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Unit-cell length a length_a	146.408 Å
Unit-cell length b length_b	146.408 Å
Unit-cell length c length_c	146.408 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	24

Space group space_group	I 21 3
Space-group number int_tables_number	199
Crystal system crystal_system	—

Resolution resolution	2.610 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2005
R_work r_work	0.1946
R_free r_free	0.2525

fit	/app/data/saxs_computation/hf/2hfg/2hfg.fit
pddf	/app/data/pr_computation/hf/2hfg/2hfg.pr.out
profile	/app/data/saxs_computation/hf/2hfg/2hfg.dat

Crystal structure of hBR3 bound to CB3s-Fab

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

CB3s Fab light chain (kappa)

State in the Current Structure

Other States of the Same Protein in the Database

CB3s Fab heavy chain

State in the Current Structure

Other States of the Same Protein in the Database

Tumor necrosis factor receptor superfamily member 13C

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

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (5 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)