SAXSdb — 4v46

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

Tumor necrosis factor ligand superfamily member 13B

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 × 120 PDB declaration: 120-meric（120） Consistent with protein copy count	Chain A0； UniProt 138–285 Chain A1； UniProt 138–285 Chain A2； UniProt 138–285 Chain A3； UniProt 138–285 Chain A4； UniProt 138–285 Chain A5； UniProt 138–285 Chain A6； UniProt 138–285 Chain A7； UniProt 138–285 Chain A8； UniProt 138–285 Chain A9； UniProt 138–285 Chain AA； UniProt 138–285 Chain AB； UniProt 138–285 Chain AC； UniProt 138–285 Chain AD； UniProt 138–285 Chain AE； UniProt 138–285 Chain AF； UniProt 138–285 Chain AG； UniProt 138–285 Chain AH； UniProt 138–285 Chain AI； UniProt 138–285 Chain AJ； UniProt 138–285 Chain AK； UniProt 138–285 Chain AL； UniProt 138–285 Chain AM； UniProt 138–285 Chain AN； UniProt 138–285 Chain AO； UniProt 138–285 Chain AP； UniProt 138–285 Chain AQ； UniProt 138–285 Chain AR； UniProt 138–285 Chain AS； UniProt 138–285 Chain AT； UniProt 138–285 Chain AU； UniProt 138–285 Chain AV； UniProt 138–285 Chain AW； UniProt 138–285 Chain AX； UniProt 138–285 Chain AY； UniProt 138–285 Chain AZ； UniProt 138–285 Chain Aa； UniProt 138–285 Chain Ab； UniProt 138–285 Chain Ac； UniProt 138–285 Chain Ad； UniProt 138–285 Chain Ae； UniProt 138–285 Chain Af； UniProt 138–285 Chain Ag； UniProt 138–285 Chain Ah； UniProt 138–285 Chain Ai； UniProt 138–285 Chain Aj； UniProt 138–285 Chain Ak； UniProt 138–285 Chain Al； UniProt 138–285 Chain Am； UniProt 138–285 Chain An； UniProt 138–285 Chain Ao； UniProt 138–285 Chain Ap； UniProt 138–285 Chain Aq； UniProt 138–285 Chain Ar； UniProt 138–285 Chain As； UniProt 138–285 Chain At； UniProt 138–285 Chain Au； UniProt 138–285 Chain Av； UniProt 138–285 Chain Aw； UniProt 138–285 Chain Ax； UniProt 138–285	Fragment：residues 138-285	Tumor necrosis factor receptor superfamily member 13C × 60 （Q96RJ3） 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

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 4V46	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1JH5 Crystal Structure of sTALL-1 of TNF family ligand Deposited 2001-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 142–285（144 aa） Fragment：sTALL-1, soluble part of TALL-1 Chain B 142–285（144 aa） Fragment：sTALL-1, soluble part of TALL-1 Chain C 142–285（144 aa） Fragment：sTALL-1, soluble part of TALL-1 Chain D 142–285（144 aa） Fragment：sTALL-1, soluble part of TALL-1 Chain E 142–285（144 aa） Fragment：sTALL-1, soluble part of TALL-1 Chain F 142–285（144 aa） Fragment：sTALL-1, soluble part of TALL-1 Chain G 142–285（144 aa） Fragment：sTALL-1, soluble part of TALL-1 Chain H 142–285（144 aa） Fragment：sTALL-1, soluble part of TALL-1 Chain I 142–285（144 aa） Fragment：sTALL-1, soluble part of TALL-1 Chain J 142–285（144 aa） Fragment：sTALL-1, soluble part of TALL-1	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；277 K；35% dioxane, pH 9.0, VAPOR DIFFUSION, HANGING DROP at 277K	Resolution 3.00 Å R-free 0.252
1KD7 Crystal structure of an extracellular domain fragment of human BAFF Deposited 2001-11-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 122–285（164 aa） Fragment：Extracellular domain fragment Chain B 122–285（164 aa） Fragment：Extracellular domain fragment Chain C 122–285（164 aa） Fragment：Extracellular domain fragment	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；8% PEG 4000, 0.1 M sodium acetatesolution of 8% PEG 4000, 0.1 M sodium acetate pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.250
1KD7 Crystal structure of an extracellular domain fragment of human BAFF Deposited 2001-11-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain K 122–285（164 aa） Fragment：Extracellular domain fragment Chain L 122–285（164 aa） Fragment：Extracellular domain fragment Chain M 122–285（164 aa） Fragment：Extracellular domain fragment	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；8% PEG 4000, 0.1 M sodium acetatesolution of 8% PEG 4000, 0.1 M sodium acetate pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.250
1KXG The 2.0 Ang Resolution Structure of BLyS, B Lymphocyte Stimulator. Deposited 2002-01-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 134–285（152 aa） Fragment：soluble portion (residues 134-285) Chain B 134–285（152 aa） Fragment：soluble portion (residues 134-285) Chain C 134–285（152 aa） Fragment：soluble portion (residues 134-285)	Not recorded	MG MAGNESIUM ION × 4 CIT CITRIC ACID × 1 DIO 1,4-DIETHYLENE DIOXIDE × 13	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；279 K；25% dioxane, 25 mM MgCl2, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 279.0K	Resolution 2.00 Å R-free 0.209
1KXG The 2.0 Ang Resolution Structure of BLyS, B Lymphocyte Stimulator. Deposited 2002-01-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 134–285（152 aa） Fragment：soluble portion (residues 134-285) Chain E 134–285（152 aa） Fragment：soluble portion (residues 134-285) Chain F 134–285（152 aa） Fragment：soluble portion (residues 134-285)	Not recorded	MG MAGNESIUM ION × 3 CIT CITRIC ACID × 1 DIO 1,4-DIETHYLENE DIOXIDE × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；279 K；25% dioxane, 25 mM MgCl2, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 279.0K	Resolution 2.00 Å R-free 0.209
1OQD Crystal structure of sTALL-1 and BCMA Deposited 2003-03-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 108 PDB declaration: 108-meric	Chain A 142–285（144 aa） Fragment：extracellular domain Chain B 142–285（144 aa） Fragment：extracellular domain Chain C 142–285（144 aa） Fragment：extracellular domain Chain D 142–285（144 aa） Fragment：extracellular domain Chain E 142–285（144 aa） Fragment：extracellular domain Chain F 142–285（144 aa） Fragment：extracellular domain Chain G 142–285（144 aa） Fragment：extracellular domain Chain H 142–285（144 aa） Fragment：extracellular domain Chain I 142–285（144 aa） Fragment：extracellular domain Chain J 142–285（144 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；277 K；dioxane, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.60 Å R-free 0.260
1OQE Crystal structure of sTALL-1 with BAFF-R Deposited 2003-03-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 108 PDB declaration: 108-meric	Chain A 142–285（144 aa） Fragment：extracellular domain Chain B 142–285（144 aa） Fragment：extracellular domain Chain C 142–285（144 aa） Fragment：extracellular domain Chain D 142–285（144 aa） Fragment：extracellular domain Chain E 142–285（144 aa） Fragment：extracellular domain Chain F 142–285（144 aa） Fragment：extracellular domain Chain G 142–285（144 aa） Fragment：extracellular domain Chain H 142–285（144 aa） Fragment：extracellular domain Chain I 142–285（144 aa） Fragment：extracellular domain Chain J 142–285（144 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
1OSG Complex between BAFF and a BR3 derived peptide presented in a beta-hairpin scaffold Deposited 2003-03-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 82–285（204 aa） Fragment：TNF domain Chain B 82–285（204 aa） Fragment：TNF domain Chain C 82–285（204 aa） Fragment：TNF domain	Not recorded	MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.7；292 K；20% PEG 3350, 1.0 M LiCl, 0.1M sodium cacodylate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 3.00 Å R-free 0.286
1OSG Complex between BAFF and a BR3 derived peptide presented in a beta-hairpin scaffold Deposited 2003-03-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 82–285（204 aa） Fragment：TNF domain Chain E 82–285（204 aa） Fragment：TNF domain Chain F 82–285（204 aa） Fragment：TNF domain	Not recorded	MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.7；292 K；20% PEG 3350, 1.0 M LiCl, 0.1M sodium cacodylate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 3.00 Å R-free 0.286
3V56 Re-refinement of PDB entry 1OSG - Complex between BAFF and a BR3 derived peptide presented in a beta-hairpin scaffold - reveals an additonal copy of the peptide. Deposited 2011-12-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 82–285（204 aa） Chain B 82–285（204 aa） Chain C 82–285（204 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.00 Å R-free 0.200
3V56 Re-refinement of PDB entry 1OSG - Complex between BAFF and a BR3 derived peptide presented in a beta-hairpin scaffold - reveals an additonal copy of the peptide. Deposited 2011-12-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 82–285（204 aa） Chain E 82–285（204 aa） Chain F 82–285（204 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.00 Å R-free 0.200
4ZCH Single-chain human APRIL-BAFF-BAFF Heterotrimer Deposited 2015-04-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 140–285（146 aa）	Not recorded	144 TRIS-HYDROXYMETHYL-METHYL-AMMONIUM × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；RESERVOIR SOLUTION : 14% PEG6000 , 1M LiCL , TRIS-HCL pH 8.50	Resolution 2.43 Å R-free 0.234
4ZCH Single-chain human APRIL-BAFF-BAFF Heterotrimer Deposited 2015-04-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain B 140–285（146 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；RESERVOIR SOLUTION : 14% PEG6000 , 1M LiCL , TRIS-HCL pH 8.50	Resolution 2.43 Å R-free 0.234
5Y9J BAFF in complex with belimumab Deposited 2017-08-25	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 A 134–285（152 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；293 K；0.1 M Tris(hydroxymethyl)aminomethane pH 8.5, 20% (w/v)polyethylene glycol 1,000	Resolution 2.05 Å R-free 0.217
6FXN Crystal structure of human BAFF in complex with Fab fragment of anti-BAFF antibody belimumab Deposited 2018-03-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 134–285（152 aa） Chain B 134–285（152 aa） Chain C 134–285（152 aa）	Mutation：H218A Mutation：H218A Mutation：H218A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；9% (w/v) PEG4000, 0.1 M MgCl2, 0.1 M HEPES pH 7.5	Resolution 2.90 Å R-free 0.231
6FXN Crystal structure of human BAFF in complex with Fab fragment of anti-BAFF antibody belimumab Deposited 2018-03-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain J 134–285（152 aa） Chain K 134–285（152 aa） Chain L 134–285（152 aa）	Mutation：H218A Mutation：H218A Mutation：H218A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；9% (w/v) PEG4000, 0.1 M MgCl2, 0.1 M HEPES pH 7.5	Resolution 2.90 Å R-free 0.231
8ZUJ Pentagonal cluster of BAFF-BAFFR ectodomain complex Deposited 2024-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain D 134–285（152 aa） Chain E 134–285（152 aa） Chain F 134–285（152 aa） Chain J 134–285（152 aa） Chain K 134–285（152 aa） Chain L 134–285（152 aa） Chain P 134–285（152 aa） Chain Q 134–285（152 aa） Chain R 134–285（152 aa） Chain V 134–285（152 aa） Chain W 134–285（152 aa） Chain X 134–285（152 aa） Chain b 134–285（152 aa） Chain c 134–285（152 aa） Chain d 134–285（152 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

11 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	T13B_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A0； PDBConstruct 1–148； UniProt 138–285 Author chain A1； PDBConstruct 1–148； UniProt 138–285 Author chain A2； PDBConstruct 1–148； UniProt 138–285 Author chain A3； PDBConstruct 1–148； UniProt 138–285 Author chain A4； PDBConstruct 1–148； UniProt 138–285 Author chain A5； PDBConstruct 1–148； UniProt 138–285 Author chain A6； PDBConstruct 1–148； UniProt 138–285 Author chain A7； PDBConstruct 1–148； UniProt 138–285 Author chain A8； PDBConstruct 1–148； UniProt 138–285 Author chain A9； PDBConstruct 1–148； UniProt 138–285 Author chain AA； PDBConstruct 1–148； UniProt 138–285 Author chain AB； PDBConstruct 1–148； UniProt 138–285 Author chain AC； PDBConstruct 1–148； UniProt 138–285 Author chain AD； PDBConstruct 1–148； UniProt 138–285 Author chain AE； PDBConstruct 1–148； UniProt 138–285 Author chain AF； PDBConstruct 1–148； UniProt 138–285 Author chain AG； PDBConstruct 1–148； UniProt 138–285 Author chain AH； PDBConstruct 1–148； UniProt 138–285 Author chain AI； PDBConstruct 1–148； UniProt 138–285 Author chain AJ； PDBConstruct 1–148； UniProt 138–285 Author chain AK； PDBConstruct 1–148； UniProt 138–285 Author chain AL； PDBConstruct 1–148； UniProt 138–285 Author chain AM； PDBConstruct 1–148； UniProt 138–285 Author chain AN； PDBConstruct 1–148； UniProt 138–285 Author chain AO； PDBConstruct 1–148； UniProt 138–285 Author chain AP； PDBConstruct 1–148； UniProt 138–285 Author chain AQ； PDBConstruct 1–148； UniProt 138–285 Author chain AR； PDBConstruct 1–148； UniProt 138–285 Author chain AS； PDBConstruct 1–148； UniProt 138–285 Author chain AT； PDBConstruct 1–148； UniProt 138–285 Author chain AU； PDBConstruct 1–148； UniProt 138–285 Author chain AV； PDBConstruct 1–148； UniProt 138–285 Author chain AW； PDBConstruct 1–148； UniProt 138–285 Author chain AX； PDBConstruct 1–148； UniProt 138–285 Author chain AY； PDBConstruct 1–148； UniProt 138–285 Author chain AZ； PDBConstruct 1–148； UniProt 138–285 Author chain Aa； PDBConstruct 1–148； UniProt 138–285 Author chain Ab； PDBConstruct 1–148； UniProt 138–285 Author chain Ac； PDBConstruct 1–148； UniProt 138–285 Author chain Ad； PDBConstruct 1–148； UniProt 138–285 Author chain Ae； PDBConstruct 1–148； UniProt 138–285 Author chain Af； PDBConstruct 1–148； UniProt 138–285 Author chain Ag； PDBConstruct 1–148； UniProt 138–285 Author chain Ah； PDBConstruct 1–148； UniProt 138–285 Author chain Ai； PDBConstruct 1–148； UniProt 138–285 Author chain Aj； PDBConstruct 1–148； UniProt 138–285 Author chain Ak； PDBConstruct 1–148； UniProt 138–285 Author chain Al； PDBConstruct 1–148； UniProt 138–285 Author chain Am； PDBConstruct 1–148； UniProt 138–285 Author chain An； PDBConstruct 1–148； UniProt 138–285 Author chain Ao； PDBConstruct 1–148； UniProt 138–285 Author chain Ap； PDBConstruct 1–148； UniProt 138–285 Author chain Aq； PDBConstruct 1–148； UniProt 138–285 Author chain Ar； PDBConstruct 1–148； UniProt 138–285 Author chain As； PDBConstruct 1–148； UniProt 138–285 Author chain At； PDBConstruct 1–148； UniProt 138–285 Author chain Au； PDBConstruct 1–148； UniProt 138–285 Author chain Av； PDBConstruct 1–148； UniProt 138–285 Author chain Aw； PDBConstruct 1–148； UniProt 138–285 Author chain Ax； PDBConstruct 1–148； UniProt 138–285

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 × 120 PDB declaration: 120-meric（120） Consistent with protein copy count	Chain B0； UniProt 1–63 Chain B1； UniProt 1–63 Chain B2； UniProt 1–63 Chain B3； UniProt 1–63 Chain B4； UniProt 1–63 Chain B5； UniProt 1–63 Chain B6； UniProt 1–63 Chain B7； UniProt 1–63 Chain B8； UniProt 1–63 Chain B9； UniProt 1–63 Chain BA； UniProt 1–63 Chain BB； UniProt 1–63 Chain BC； UniProt 1–63 Chain BD； UniProt 1–63 Chain BE； UniProt 1–63 Chain BF； UniProt 1–63 Chain BG； UniProt 1–63 Chain BH； UniProt 1–63 Chain BI； UniProt 1–63 Chain BJ； UniProt 1–63 Chain BK； UniProt 1–63 Chain BL； UniProt 1–63 Chain BM； UniProt 1–63 Chain BN； UniProt 1–63 Chain BO； UniProt 1–63 Chain BP； UniProt 1–63 Chain BQ； UniProt 1–63 Chain BR； UniProt 1–63 Chain BS； UniProt 1–63 Chain BT； UniProt 1–63 Chain BU； UniProt 1–63 Chain BV； UniProt 1–63 Chain BW； UniProt 1–63 Chain BX； UniProt 1–63 Chain BY； UniProt 1–63 Chain BZ； UniProt 1–63 Chain Ba； UniProt 1–63 Chain Bb； UniProt 1–63 Chain Bc； UniProt 1–63 Chain Bd； UniProt 1–63 Chain Be； UniProt 1–63 Chain Bf； UniProt 1–63 Chain Bg； UniProt 1–63 Chain Bh； UniProt 1–63 Chain Bi； UniProt 1–63 Chain Bj； UniProt 1–63 Chain Bk； UniProt 1–63 Chain Bl； UniProt 1–63 Chain Bm； UniProt 1–63 Chain Bn； UniProt 1–63 Chain Bo； UniProt 1–63 Chain Bp； UniProt 1–63 Chain Bq； UniProt 1–63 Chain Br； UniProt 1–63 Chain Bs； UniProt 1–63 Chain Bt； UniProt 1–63 Chain Bu； UniProt 1–63 Chain Bv； UniProt 1–63 Chain Bw； UniProt 1–63 Chain Bx； UniProt 1–63	Fragment：residues 1-63	Tumor necrosis factor ligand superfamily member 13B × 60 （Q9Y275） 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

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 4V46	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 ligand/ion 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 ligand/ion 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 ligand/ion 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
2HFG Crystal structure of hBR3 bound to CB3s-Fab Deposited 2006-06-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain R 7–54（48 aa） Fragment：cysteine rich domain (residues 7-54)	Mutation：V20N, L27P	No recorded non-water small molecule	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
8ZUJ Pentagonal cluster of BAFF-BAFFR ectodomain complex Deposited 2024-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion 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 ligand/ion 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	2
Chains and sequence ranges	Author chain B0； PDBConstruct 1–63； UniProt 1–63 Author chain B1； PDBConstruct 1–63； UniProt 1–63 Author chain B2； PDBConstruct 1–63； UniProt 1–63 Author chain B3； PDBConstruct 1–63； UniProt 1–63 Author chain B4； PDBConstruct 1–63； UniProt 1–63 Author chain B5； PDBConstruct 1–63； UniProt 1–63 Author chain B6； PDBConstruct 1–63； UniProt 1–63 Author chain B7； PDBConstruct 1–63； UniProt 1–63 Author chain B8； PDBConstruct 1–63； UniProt 1–63 Author chain B9； PDBConstruct 1–63； UniProt 1–63 Author chain BA； PDBConstruct 1–63； UniProt 1–63 Author chain BB； PDBConstruct 1–63； UniProt 1–63 Author chain BC； PDBConstruct 1–63； UniProt 1–63 Author chain BD； PDBConstruct 1–63； UniProt 1–63 Author chain BE； PDBConstruct 1–63； UniProt 1–63 Author chain BF； PDBConstruct 1–63； UniProt 1–63 Author chain BG； PDBConstruct 1–63； UniProt 1–63 Author chain BH； PDBConstruct 1–63； UniProt 1–63 Author chain BI； PDBConstruct 1–63； UniProt 1–63 Author chain BJ； PDBConstruct 1–63； UniProt 1–63 Author chain BK； PDBConstruct 1–63； UniProt 1–63 Author chain BL； PDBConstruct 1–63； UniProt 1–63 Author chain BM； PDBConstruct 1–63； UniProt 1–63 Author chain BN； PDBConstruct 1–63； UniProt 1–63 Author chain BO； PDBConstruct 1–63； UniProt 1–63 Author chain BP； PDBConstruct 1–63； UniProt 1–63 Author chain BQ； PDBConstruct 1–63； UniProt 1–63 Author chain BR； PDBConstruct 1–63； UniProt 1–63 Author chain BS； PDBConstruct 1–63； UniProt 1–63 Author chain BT； PDBConstruct 1–63； UniProt 1–63 Author chain BU； PDBConstruct 1–63； UniProt 1–63 Author chain BV； PDBConstruct 1–63； UniProt 1–63 Author chain BW； PDBConstruct 1–63； UniProt 1–63 Author chain BX； PDBConstruct 1–63； UniProt 1–63 Author chain BY； PDBConstruct 1–63； UniProt 1–63 Author chain BZ； PDBConstruct 1–63； UniProt 1–63 Author chain Ba； PDBConstruct 1–63； UniProt 1–63 Author chain Bb； PDBConstruct 1–63； UniProt 1–63 Author chain Bc； PDBConstruct 1–63； UniProt 1–63 Author chain Bd； PDBConstruct 1–63； UniProt 1–63 Author chain Be； PDBConstruct 1–63； UniProt 1–63 Author chain Bf； PDBConstruct 1–63； UniProt 1–63 Author chain Bg； PDBConstruct 1–63； UniProt 1–63 Author chain Bh； PDBConstruct 1–63； UniProt 1–63 Author chain Bi； PDBConstruct 1–63； UniProt 1–63 Author chain Bj； PDBConstruct 1–63； UniProt 1–63 Author chain Bk； PDBConstruct 1–63； UniProt 1–63 Author chain Bl； PDBConstruct 1–63； UniProt 1–63 Author chain Bm； PDBConstruct 1–63； UniProt 1–63 Author chain Bn； PDBConstruct 1–63； UniProt 1–63 Author chain Bo； PDBConstruct 1–63； UniProt 1–63 Author chain Bp； PDBConstruct 1–63； UniProt 1–63 Author chain Bq； PDBConstruct 1–63； UniProt 1–63 Author chain Br； PDBConstruct 1–63； UniProt 1–63 Author chain Bs； PDBConstruct 1–63； UniProt 1–63 Author chain Bt； PDBConstruct 1–63； UniProt 1–63 Author chain Bu； PDBConstruct 1–63； UniProt 1–63 Author chain Bv； PDBConstruct 1–63； UniProt 1–63 Author chain Bw； PDBConstruct 1–63； UniProt 1–63 Author chain Bx； PDBConstruct 1–63； UniProt 1–63

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	4v46
Deposition date deposition_date	2003-03-23
Structure title title	Crystal structure of the BAFF-BAFF-R complex
Keywords keywords	Cytokine; CYTOKINE
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	76.79 Å
Radius of gyration Rg (electron density) rg_electron	75.31 Å
Forward intensity I(0) i0	16389200000.00
Molecular weight molecular_weight	1135300.0 kDa
Excluded volume excluded_volume	1438100 Å³
Envelope volume envelope_volume	2290500 Å³
Hydration-shell volume shell_volume	239910 Å³
Envelope diameter envelope_diameter	204.6 Å
Shell Rg shell_rg	89.45 Å
Envelope Rg envelope_rg	70.09 Å
Shape Rg shape_rg	75.23 Å
Total Rg total_rg	75.75 Å
Total atoms total_atoms	79720
Residues n_residues	10140
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	192.1 Å
Rg (real space) rg_real	76.15 Å
Rg uncertainty (real space) rg_real_error	0.36 Å
I(0) (real space) i0_real	1.6390e+10
I(0) uncertainty (real space) i0_real_error	2.7410e+08
Rg (reciprocal space) rg_reciprocal	78.93 Å
I(0) (reciprocal space) i0_reciprocal	16480000000.0000
Solution quality estimate total_estimate	0.8399
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	115.3 Å
Skewness Skewness skewness	-0.271
Kurtosis Kurtosis kurtosis	-0.572
Angular range angular_range	— – 0.1000 Å⁻¹
Current regularization parameter α current_alpha	0.0008
Highest regularization parameter α highest_alpha	5186000000.0000
Real-space data points n_real_points	21
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.976; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.000

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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	Tumor necrosis factor ligand superfamily member 13B
Molecular weight formula_weight	16701.1 kDa
Source method src_method	man
Copy count entity_count	60

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;AA,AB,AC,AD,AE,AF,AG,AH,AI,AJ,AK,AL,AM,AN,AO,AP,AQ,AR,AS,AT,AU,AV,AW,AX,AY,AZ,A0,A1,A2,A3,A4,A5,A6,A7,A8,A9,Aa,Ab,Ac,Ad,Ae,Af,Ag,Ah,Ai,Aj,Ak,Al,Am,An,Ao,Ap,Aq,Ar,As,At,Au,Av,Aw,Ax ;
Atom count atom_count	79720

PEETVTQDCLQLIADSETPTIQKGSYTFVPWLLSFKRGSALEEKENKILVKETGYFFIYGQVLYTDKTYAMGHLIQRKKVHVFGDELSLVTLFRCIQNMPETLPNNSCYSAGIAKLEEGDELQLAIPRENAQISLDGDVTFFGALKLL

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	Spodoptera frugiperda

Entity 2 Entity 2 polymer

Description description	Tumor necrosis factor receptor superfamily member 13C
Molecular weight formula_weight	6727.9 kDa
Source method src_method	man
Copy count entity_count	60

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;BA,BB,BC,BD,BE,BF,BG,BH,BI,BJ,BK,BL,BM,BN,BO,BP,BQ,BR,BS,BT,BU,BV,BW,BX,BY,BZ,B0,B1,B2,B3,B4,B5,B6,B7,B8,B9,Ba,Bb,Bc,Bd,Be,Bf,Bg,Bh,Bi,Bj,Bk,Bl,Bm,Bn,Bo,Bp,Bq,Br,Bs,Bt,Bu,Bv,Bw,Bx ;

MRRGPRSLRGRDAPAPTPCVPAECFDLLVRHCVACGLLRTPRPKPAGASSPAPRTALQPQESV

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	Spodoptera frugiperda

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	40

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8. Citations (1)

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Unit-cell length a length_a	175.500 Å
Unit-cell length b length_b	194.800 Å
Unit-cell length c length_c	274.400 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	93.30 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	120

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	3.300 Å
Low-resolution limit resolution_low	19.950 Å
R factor r_factor	—
R_work r_work	0.2180
R_free r_free	0.2260

fit	/app/data/saxs_computation/v4/4v46/4v46.fit
pddf	/app/data/pr_computation/v4/4v46/4v46.pr.out
profile	/app/data/saxs_computation/v4/4v46/4v46.dat

Crystal structure of the BAFF-BAFF-R complex

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

Tumor necrosis factor ligand superfamily member 13B

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 (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 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)