9pbh

AS19.2 TCR complex with PSG5-HLA B*27:05

Method: X-RAY DIFFRACTION Dmax: 135.2 Å Quality: GOOD

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

MHC class I antigen

Homo sapiens

UniProt A3F718

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 11–288 Not recorded Beta-2-microglobulin × 1 (P61769) Pregnancy-specific beta-1-glycoprotein 5 × 1 (Q15238) TCR19.2 alpha chain × 1 TCR 19.2 beta chain × 1 GOL GLYCEROL × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;0.2 M sodium formate; 20% PEG 3350 Resolution 2.13 Å R-free 0.246

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.

17 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A3F718_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–279; UniProt 11–288

Beta-2-microglobulin

Homo sapiens

UniProt P61769

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 21–119 Not recorded MHC class I antigen × 1 (A3F718) Pregnancy-specific beta-1-glycoprotein 5 × 1 (Q15238) TCR19.2 alpha chain × 1 TCR 19.2 beta chain × 1 GOL GLYCEROL × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;0.2 M sodium formate; 20% PEG 3350 Resolution 2.13 Å R-free 0.246

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.

1313 other PDB entries and 1998 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–100; UniProt 21–119

Pregnancy-specific beta-1-glycoprotein 5

OrganismNot specified

UniProt Q15238

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 C; UniProt 327–335 Not recorded MHC class I antigen × 1 (A3F718) Beta-2-microglobulin × 1 (P61769) TCR19.2 alpha chain × 1 TCR 19.2 beta chain × 1 GOL GLYCEROL × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;0.2 M sodium formate; 20% PEG 3350 Resolution 2.13 Å R-free 0.246

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name PSG5_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–9; UniProt 327–335

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 9pbh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9pbh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9pbh
Deposition date deposition_date2025-06-26
Structure title titleAS19.2 TCR complex with PSG5-HLA B*27:05
Keywords keywordsTCR, complex, 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_guinier37.84
Radius of gyration Rg (electron density) rg_electron38.22
Forward intensity I(0) i0146766000.00
Molecular weight molecular_weight94708.0 kDa
Excluded volume excluded_volume117170 ų
Envelope volume envelope_volume159330 ų
Hydration-shell volume shell_volume38248 ų
Envelope diameter envelope_diameter141.2
Shell Rg shell_rg39.37
Envelope Rg envelope_rg38.56
Shape Rg shape_rg38.23
Total Rg total_rg38.28
Total atoms total_atoms6684
Residues n_residues832
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 dmax135.2
Rg (real space) rg_real38.48
Rg uncertainty (real space) rg_real_error1.87
I(0) (real space) i0_real1.4680e+08
I(0) uncertainty (real space) i0_real_error2.5460e+06
Rg (reciprocal space) rg_reciprocal38.08
I(0) (reciprocal space) i0_reciprocal146700000.0000
Solution quality estimate total_estimate0.7740
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.2
Skewness Skewness skewness0.665
Kurtosis Kurtosis kurtosis-0.177
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18010000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.576; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.649; Smooth: 0.684

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)