1xu2

The crystal structure of APRIL bound to BCMA

Method: X-RAY DIFFRACTION Dmax: 73.3 Å Quality: GOOD

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

Tumor necrosis factor ligand superfamily member 13

Mus musculus

UniProt Q9D777

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 104–241 Chain B; UniProt 104–241 Chain D; UniProt 104–241 Fragment:TNF domain of APRIL Tumor necrosis factor receptor superfamily member 17 × 3 (Q02223) 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

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TNF13_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–138; UniProt 104–241 Author chain B; PDBConstruct 1–138; UniProt 104–241 Author chain D; PDBConstruct 1–138; UniProt 104–241

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain R; UniProt 5–51 Chain S; UniProt 5–51 Chain T; UniProt 5–51 Fragment:BCMA ECD Tumor necrosis factor ligand superfamily member 13 × 3 (Q9D777) 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

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.

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 R; PDBConstruct 1–47; UniProt 5–51 Author chain S; PDBConstruct 1–47; UniProt 5–51 Author chain T; PDBConstruct 1–47; UniProt 5–51

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

SAXS profile for 1xu2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1xu2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1xu2
Deposition date deposition_date2004-10-25
Structure title titleThe crystal structure of APRIL bound to BCMA
Keywords keywordsTNFSF, cytokine, CRD, receptor, jelly-roll, cysteine-rich, HORMONE-GROWTH FACTOR receptor COMPLEX; CYTOKINE, HORMONE/GROWTH FACTOR receptor
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier23.86
Radius of gyration Rg (electron density) rg_electron22.35
Forward intensity I(0) i058288800.00
Molecular weight molecular_weight58258.0 kDa
Excluded volume excluded_volume72410 ų
Envelope volume envelope_volume84734 ų
Hydration-shell volume shell_volume30128 ų
Envelope diameter envelope_diameter77.2
Shell Rg shell_rg30.59
Envelope Rg envelope_rg22.86
Shape Rg shape_rg22.32
Total Rg total_rg23.34
Total atoms total_atoms4083
Residues n_residues519
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax73.3
Rg (real space) rg_real23.68
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real5.8290e+07
I(0) uncertainty (real space) i0_real_error7.7790e+05
Rg (reciprocal space) rg_reciprocal23.72
I(0) (reciprocal space) i0_reciprocal58290000.0000
Solution quality estimate total_estimate0.8200
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary30.9
Skewness Skewness skewness0.100
Kurtosis Kurtosis kurtosis-0.468
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13980000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1xu2a_
Class classb — All beta proteins
Fold Fold foldb.22 — TNF-like
Superfamily Superfamily superfamilyb.22.1 — TNF-like
Family Family familyb.22.1.1 — TNF-like
Domain ID domain_idd1xu2b_
Class classb — All beta proteins
Fold Fold foldb.22 — TNF-like
Superfamily Superfamily superfamilyb.22.1 — TNF-like
Family Family familyb.22.1.1 — TNF-like
Domain ID domain_idd1xu2d_
Class classb — All beta proteins
Fold Fold foldb.22 — TNF-like
Superfamily Superfamily superfamilyb.22.1 — TNF-like
Family Family familyb.22.1.1 — TNF-like
Domain ID domain_idd1xu2r_
Class classg — Small proteins
Fold Fold foldg.24 — TNF receptor-like
Superfamily Superfamily superfamilyg.24.1 — TNF receptor-like
Family Family familyg.24.1.2 — BAFF receptor-like
Domain ID domain_idd1xu2s_
Class classg — Small proteins
Fold Fold foldg.24 — TNF receptor-like
Superfamily Superfamily superfamilyg.24.1 — TNF receptor-like
Family Family familyg.24.1.2 — BAFF receptor-like
Domain ID domain_idd1xu2t_
Class classg — Small proteins
Fold Fold foldg.24 — TNF receptor-like
Superfamily Superfamily superfamilyg.24.1 — TNF receptor-like
Family Family familyg.24.1.2 — BAFF receptor-like

CATH v4.4 (3 domains)

Domain ID domain_id1xu2A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily40
Domain ID domain_id1xu2B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily40
Domain ID domain_id1xu2D00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)