1oqd

Crystal structure of sTALL-1 and BCMA

Method: X-RAY DIFFRACTION D_max: 148.7 Å Quality: REASONABLE

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

Tumor necrosis factor ligand superfamily member 13B, soluble form

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 × 108 PDB declaration: 108-meric（108） Consistent with protein copy count	Chain A； UniProt 142–285 Chain B； UniProt 142–285 Chain C； UniProt 142–285 Chain D； UniProt 142–285 Chain E； UniProt 142–285 Chain F； UniProt 142–285 Chain G； UniProt 142–285 Chain H； UniProt 142–285 Chain I； UniProt 142–285 Chain J； UniProt 142–285	Fragment：extracellular domain	Tumor necrosis factor receptor superfamily member 17 × 48 （Q02223）	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

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 1OQD	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 oligomeric state 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 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 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
1OQE Crystal structure of sTALL-1 with BAFF-R Deposited 2003-03-07	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
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 A0 138–285（148 aa） Fragment：residues 138-285 Chain A1 138–285（148 aa） Fragment：residues 138-285 Chain A2 138–285（148 aa） Fragment：residues 138-285 Chain A3 138–285（148 aa） Fragment：residues 138-285 Chain A4 138–285（148 aa） Fragment：residues 138-285 Chain A5 138–285（148 aa） Fragment：residues 138-285 Chain A6 138–285（148 aa） Fragment：residues 138-285 Chain A7 138–285（148 aa） Fragment：residues 138-285 Chain A8 138–285（148 aa） Fragment：residues 138-285 Chain A9 138–285（148 aa） Fragment：residues 138-285 Chain AA 138–285（148 aa） Fragment：residues 138-285 Chain AB 138–285（148 aa） Fragment：residues 138-285 Chain AC 138–285（148 aa） Fragment：residues 138-285 Chain AD 138–285（148 aa） Fragment：residues 138-285 Chain AE 138–285（148 aa） Fragment：residues 138-285 Chain AF 138–285（148 aa） Fragment：residues 138-285 Chain AG 138–285（148 aa） Fragment：residues 138-285 Chain AH 138–285（148 aa） Fragment：residues 138-285 Chain AI 138–285（148 aa） Fragment：residues 138-285 Chain AJ 138–285（148 aa） Fragment：residues 138-285 Chain AK 138–285（148 aa） Fragment：residues 138-285 Chain AL 138–285（148 aa） Fragment：residues 138-285 Chain AM 138–285（148 aa） Fragment：residues 138-285 Chain AN 138–285（148 aa） Fragment：residues 138-285 Chain AO 138–285（148 aa） Fragment：residues 138-285 Chain AP 138–285（148 aa） Fragment：residues 138-285 Chain AQ 138–285（148 aa） Fragment：residues 138-285 Chain AR 138–285（148 aa） Fragment：residues 138-285 Chain AS 138–285（148 aa） Fragment：residues 138-285 Chain AT 138–285（148 aa） Fragment：residues 138-285 Chain AU 138–285（148 aa） Fragment：residues 138-285 Chain AV 138–285（148 aa） Fragment：residues 138-285 Chain AW 138–285（148 aa） Fragment：residues 138-285 Chain AX 138–285（148 aa） Fragment：residues 138-285 Chain AY 138–285（148 aa） Fragment：residues 138-285 Chain AZ 138–285（148 aa） Fragment：residues 138-285 Chain Aa 138–285（148 aa） Fragment：residues 138-285 Chain Ab 138–285（148 aa） Fragment：residues 138-285 Chain Ac 138–285（148 aa） Fragment：residues 138-285 Chain Ad 138–285（148 aa） Fragment：residues 138-285 Chain Ae 138–285（148 aa） Fragment：residues 138-285 Chain Af 138–285（148 aa） Fragment：residues 138-285 Chain Ag 138–285（148 aa） Fragment：residues 138-285 Chain Ah 138–285（148 aa） Fragment：residues 138-285 Chain Ai 138–285（148 aa） Fragment：residues 138-285 Chain Aj 138–285（148 aa） Fragment：residues 138-285 Chain Ak 138–285（148 aa） Fragment：residues 138-285 Chain Al 138–285（148 aa） Fragment：residues 138-285 Chain Am 138–285（148 aa） Fragment：residues 138-285 Chain An 138–285（148 aa） Fragment：residues 138-285 Chain Ao 138–285（148 aa） Fragment：residues 138-285 Chain Ap 138–285（148 aa） Fragment：residues 138-285 Chain Aq 138–285（148 aa） Fragment：residues 138-285 Chain Ar 138–285（148 aa） Fragment：residues 138-285 Chain As 138–285（148 aa） Fragment：residues 138-285 Chain At 138–285（148 aa） Fragment：residues 138-285 Chain Au 138–285（148 aa） Fragment：residues 138-285 Chain Av 138–285（148 aa） Fragment：residues 138-285 Chain Aw 138–285（148 aa） Fragment：residues 138-285 Chain Ax 138–285（148 aa） Fragment：residues 138-285	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
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 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 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 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 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 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	TN13B_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–144； UniProt 142–285 Author chain B； PDBConstruct 1–144； UniProt 142–285 Author chain C； PDBConstruct 1–144； UniProt 142–285 Author chain D； PDBConstruct 1–144； UniProt 142–285 Author chain E； PDBConstruct 1–144； UniProt 142–285 Author chain F； PDBConstruct 1–144； UniProt 142–285 Author chain G； PDBConstruct 1–144； UniProt 142–285 Author chain H； PDBConstruct 1–144； UniProt 142–285 Author chain I； PDBConstruct 1–144； UniProt 142–285 Author chain J； PDBConstruct 1–144； UniProt 142–285

Tumor necrosis factor receptor superfamily member 17

Homo sapiens

UniProt Q02223

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 × 108 PDB declaration: 108-meric（108） Consistent with protein copy count	Chain K； UniProt 8–46 Chain L； UniProt 8–46 Chain M； UniProt 8–46 Chain N； UniProt 8–46 Chain O； UniProt 8–46 Chain P； UniProt 8–46 Chain Q； UniProt 8–46 Chain R； UniProt 8–46	Fragment：extracellular domain	Tumor necrosis factor ligand superfamily member 13B, soluble form × 60 （Q9Y275）	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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 1OQD	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1XU2 The crystal structure of APRIL bound to BCMA Deposited 2004-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain R 5–51（47 aa） Fragment：BCMA ECD Chain S 5–51（47 aa） Fragment：BCMA ECD Chain T 5–51（47 aa） Fragment：BCMA ECD	Not recorded	NI NICKEL (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；292 K；well solution: 0.1M MES, 5% Peg 8000, 10% Peg 1000, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.35 Å R-free 0.213
2KN1 Solution NMR Structure of BCMA Deposited 2009-08-11	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 2–50（49 aa） Fragment：residues 2-50	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；Ionic strength (raw mmCIF value) 10；Pressure ambient NMR sample composition 900 uM BCMA, 10 mM sodium phosphate, 0.02 % sodium azide, 95% H2O, 5% D2O \| 95% H2O/5% D2O	Resolution not provided
4ZFO J22.9-xi: chimeric mouse/human antibody against human BCMA (CD269) Deposited 2015-04-21	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 F 1–54（54 aa） Fragment：Extracellular (N-terminal) domain, UNP residues 1-54	Not recorded	CU COPPER (II) ION × 1 BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293.15 K；1 microliter of the complex at 8 mg/ml with 2 microliters of 21% PEG 3350, 0.1 M BisTris pH 6.5 and 5 mM CuCl2	Resolution 1.90 Å R-free 0.209
4ZFO J22.9-xi: chimeric mouse/human antibody against human BCMA (CD269) Deposited 2015-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 1–54（54 aa） Fragment：Extracellular (N-terminal) domain, UNP residues 1-54	Not recorded	CU COPPER (II) ION × 2 BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293.15 K；1 microliter of the complex at 8 mg/ml with 2 microliters of 21% PEG 3350, 0.1 M BisTris pH 6.5 and 5 mM CuCl2	Resolution 1.90 Å R-free 0.209
6J7W Crystal Structure of Human BCMA in complex with UniAb(TM) VH Deposited 2019-01-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 6–44（39 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；0.2M sodium malonate pH 4.0 and 20% PEG 3350	Resolution 2.60 Å R-free 0.271
6J7W Crystal Structure of Human BCMA in complex with UniAb(TM) VH Deposited 2019-01-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 6–44（39 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；0.2M sodium malonate pH 4.0 and 20% PEG 3350	Resolution 2.60 Å R-free 0.271
8HXQ Nanobody1 in complex with human BCMA ECD Deposited 2023-01-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–54（54 aa） Chain D 1–54（54 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.1；293 K；0.2 M Ammonium sulfate, 20% w/v Polyethylene glycol 3350, pH6.1	Resolution 2.40 Å R-free 0.274
8HXR Nanobody2 in complex with human BCMA ECD Deposited 2023-01-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–54（54 aa） Chain D 1–54（54 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；1.8 M Sodium acetate trihydrate, 0.1 M Bis-Tris Propane pH7.0	Resolution 2.70 Å R-free 0.287
8QY9 J22.9-H, fully humanized Fab Fragment based on chimeric J22.9-xi IgG against BCMA Deposited 2023-10-25	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 7–41（35 aa）	Not recorded	CU COPPER (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293.15 K；14% PEG 3350 100 mM BisTris 7.5 mM Cu(II)	Resolution 3.10 Å R-free 0.301
8QYA J22.9-FNY, fully humanized, CDR optimized Fab Fragment based on chimeric J22.9-xi IgG against BCMA; with VH CDR2 glycosylation Deposited 2023-10-25	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 6–41（36 aa）	Not recorded	CU COPPER (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；PEG 3350 CuCl2 BisTris	Resolution 2.72 Å R-free 0.299
8QYB J22.9-ISY, fully humanized and CDR optimized Fab Fragment based on chimeric J22.9-xi IgG against BCMA Deposited 2023-10-25	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 7–41（35 aa）	Not recorded	CU COPPER (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；14% PEG 3350 7.5 mM CuCl2 BisTris	Resolution 3.09 Å R-free 0.288
9MQO Crystal structure of BCMA in complex with CA10v2 Fab Deposited 2025-01-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: 18-meric	Chain A 1–54（54 aa） Chain D 1–54（54 aa） Chain G 1–54（54 aa） Chain J 1–54（54 aa） Chain M 1–54（54 aa） Chain P 1–54（54 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.18 M Sodium Chloride, 0.09 M Phosphate/citrate pH 4.2, 20 % w/v PEG 8000, 0.1M Sodium Malonate	Resolution 3.18 Å R-free 0.272

10 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TNR17_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain K； PDBConstruct 1–39； UniProt 8–46 Author chain L； PDBConstruct 1–39； UniProt 8–46 Author chain M； PDBConstruct 1–39； UniProt 8–46 Author chain N； PDBConstruct 1–39； UniProt 8–46 Author chain O； PDBConstruct 1–39； UniProt 8–46 Author chain P； PDBConstruct 1–39； UniProt 8–46 Author chain Q； PDBConstruct 1–39； UniProt 8–46 Author chain R； PDBConstruct 1–39； UniProt 8–46

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1oqd
Deposition date deposition_date	2003-03-07
Structure title title	Crystal structure of sTALL-1 and BCMA
Keywords keywords	ligand receptor complex, IMMUNE RESPONSE; IMMUNE RESPONSE
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	45.41 Å
Radius of gyration Rg (electron density) rg_electron	44.58 Å
Forward intensity I(0) i0	539993000.00
Molecular weight molecular_weight	195250.0 kDa
Excluded volume excluded_volume	245630 Å³
Envelope volume envelope_volume	334070 Å³
Hydration-shell volume shell_volume	62020 Å³
Envelope diameter envelope_diameter	155.7 Å
Shell Rg shell_rg	49.91 Å
Envelope Rg envelope_rg	43.87 Å
Shape Rg shape_rg	44.54 Å
Total Rg total_rg	44.98 Å
Total atoms total_atoms	13704
Residues n_residues	1734
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	148.7 Å
Rg (real space) rg_real	45.41 Å
Rg uncertainty (real space) rg_real_error	1.18 Å
I(0) (real space) i0_real	5.4000e+08
I(0) uncertainty (real space) i0_real_error	9.9660e+06
Rg (reciprocal space) rg_reciprocal	45.41 Å
I(0) (reciprocal space) i0_reciprocal	540000000.0000
Solution quality estimate total_estimate	0.6725
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	42.5 Å
Skewness Skewness skewness	0.213
Kurtosis Kurtosis kurtosis	-0.664
Angular range angular_range	— – 0.1750 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	69670000.0000
Real-space data points n_real_points	36
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.955; Smooth: 0.841

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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	Tumor necrosis factor ligand superfamily member 13B, soluble form
Molecular weight formula_weight	16244.6 kDa
Source method src_method	man
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J
Atom count atom_count	13704

VTQDCLQLIADSETPTIQKGSYTFVPWLLSFKRGSALEEKENKILVKETGYFFIYGQVLYTDKTYAMGHLIQRKKVHVFGDELSLVTLFRCIQNMPETLPNNSCYSAGIAKLEEGDELQLAIPRENAQISLDGDVTFFGALKLL

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	Tumor necrosis factor receptor superfamily member 17
Molecular weight formula_weight	4370.9 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	K,L,M,N,O,P,Q,R

CSQNEYFDSLLHACIPCQLRCSSNTPPLTCQRYCNASVT

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

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7. Fold Classification (SCOP + CATH) 28 domains

SCOP 2.08 (18 domains)

Domain ID domain_id	d1oqda_
Class class	b — All beta proteins
Fold Fold fold	b.22 — TNF-like
Superfamily Superfamily superfamily	b.22.1 — TNF-like
Family Family family	b.22.1.1 — TNF-like

Domain ID domain_id	d1oqdb_
Class class	b — All beta proteins
Fold Fold fold	b.22 — TNF-like
Superfamily Superfamily superfamily	b.22.1 — TNF-like
Family Family family	b.22.1.1 — TNF-like

Domain ID domain_id	d1oqdc_
Class class	b — All beta proteins
Fold Fold fold	b.22 — TNF-like
Superfamily Superfamily superfamily	b.22.1 — TNF-like
Family Family family	b.22.1.1 — TNF-like

Domain ID domain_id	d1oqdd_
Class class	b — All beta proteins
Fold Fold fold	b.22 — TNF-like
Superfamily Superfamily superfamily	b.22.1 — TNF-like
Family Family family	b.22.1.1 — TNF-like

Domain ID domain_id	d1oqde_
Class class	b — All beta proteins
Fold Fold fold	b.22 — TNF-like
Superfamily Superfamily superfamily	b.22.1 — TNF-like
Family Family family	b.22.1.1 — TNF-like

Domain ID domain_id	d1oqdf_
Class class	b — All beta proteins
Fold Fold fold	b.22 — TNF-like
Superfamily Superfamily superfamily	b.22.1 — TNF-like
Family Family family	b.22.1.1 — TNF-like

Domain ID domain_id	d1oqdg_
Class class	b — All beta proteins
Fold Fold fold	b.22 — TNF-like
Superfamily Superfamily superfamily	b.22.1 — TNF-like
Family Family family	b.22.1.1 — TNF-like

Domain ID domain_id	d1oqdh_
Class class	b — All beta proteins
Fold Fold fold	b.22 — TNF-like
Superfamily Superfamily superfamily	b.22.1 — TNF-like
Family Family family	b.22.1.1 — TNF-like

Domain ID domain_id	d1oqdi_
Class class	b — All beta proteins
Fold Fold fold	b.22 — TNF-like
Superfamily Superfamily superfamily	b.22.1 — TNF-like
Family Family family	b.22.1.1 — TNF-like

Domain ID domain_id	d1oqdj_
Class class	b — All beta proteins
Fold Fold fold	b.22 — TNF-like
Superfamily Superfamily superfamily	b.22.1 — TNF-like
Family Family family	b.22.1.1 — TNF-like

Domain ID domain_id	d1oqdk_
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

Domain ID domain_id	d1oqdl_
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

Domain ID domain_id	d1oqdm_
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

Domain ID domain_id	d1oqdn_
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

Domain ID domain_id	d1oqdo_
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

Domain ID domain_id	d1oqdp_
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

Domain ID domain_id	d1oqdq_
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

Domain ID domain_id	d1oqdr_
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 (10 domains)

Domain ID domain_id	1oqdA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1oqdB00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1oqdC00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1oqdD00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1oqdE00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1oqdF00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1oqdG00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1oqdH00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1oqdI00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1oqdJ00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	40 —

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8. Citations (1)

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Unit-cell length a length_a	232.854 Å
Unit-cell length b length_b	232.854 Å
Unit-cell length c length_c	212.477 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	120

Space group space_group	P 63 2 2
Space-group number int_tables_number	182
Crystal system crystal_system	—

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	19.870 Å
R factor r_factor	0.2400
R_work r_work	0.2400
R_free r_free	0.2600

fit	/app/data/saxs_computation/oq/1oqd/1oqd.fit
pddf	/app/data/pr_computation/oq/1oqd/1oqd.pr.out
profile	/app/data/saxs_computation/oq/1oqd/1oqd.dat

Crystal structure of sTALL-1 and BCMA

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

Tumor necrosis factor ligand superfamily member 13B, soluble form

State in the Current Structure

Other States of the Same Protein in the Database

Tumor necrosis factor receptor superfamily member 17

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 (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) 28 domains

SCOP 2.08 (18 domains)

CATH v4.4 (10 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)