6v13

immune receptor complex

Method: X-RAY DIFFRACTION Dmax: 129.2 Å Quality: GOOD

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

HLA class II histocompatibility antigen, DR alpha chain

Homo sapiens

UniProt P01903

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 30–206 Not recorded HLA class II histocompatibility antigen, DRB1-4 beta chain × 1 (P13760) Fibrinogen beta 74cit69-81 × 1 G08 TCR alpha chain × 1 G08 TCR beta chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GOL GLYCEROL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.2 M trisodium citrate, 20% PEG 3350 Resolution 2.75 Å R-free 0.247

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.

139 other PDB entries and 219 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DRA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–181; UniProt 30–206

HLA class II histocompatibility antigen, DRB1-4 beta chain

Homo sapiens

UniProt P13760

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 30–219 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) Fibrinogen beta 74cit69-81 × 1 G08 TCR alpha chain × 1 G08 TCR beta chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GOL GLYCEROL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.2 M trisodium citrate, 20% PEG 3350 Resolution 2.75 Å R-free 0.247

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.

32 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2B14_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–190; UniProt 30–219

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 6v13

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6v13
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6v13
Deposition date deposition_date2019-11-19
Structure title titleimmune receptor complex
Keywords keywordsImmune receptor, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.03
Radius of gyration Rg (electron density) rg_electron37.43
Forward intensity I(0) i0135286000.00
Molecular weight molecular_weight92989.0 kDa
Excluded volume excluded_volume115860 ų
Envelope volume envelope_volume153470 ų
Hydration-shell volume shell_volume37309 ų
Envelope diameter envelope_diameter139.7
Shell Rg shell_rg39.18
Envelope Rg envelope_rg37.88
Shape Rg shape_rg37.43
Total Rg total_rg37.55
Total atoms total_atoms6569
Residues n_residues811
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 dmax129.2
Rg (real space) rg_real37.57
Rg uncertainty (real space) rg_real_error1.49
I(0) (real space) i0_real1.3530e+08
I(0) uncertainty (real space) i0_real_error2.2800e+06
Rg (reciprocal space) rg_reciprocal37.24
I(0) (reciprocal space) i0_reciprocal135200000.0000
Solution quality estimate total_estimate0.7803
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.0
Skewness Skewness skewness0.640
Kurtosis Kurtosis kurtosis-0.163
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16200000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.682; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.552; Smooth: 0.544

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)