8xkc

The structure of HLA-A/Pep16

Method: X-RAY DIFFRACTION Dmax: 75.9 Å Quality: EXCELLENT

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

HLA class I heavy chain

Homo sapiens

UniProt Q5SPM2

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 25–298 Not recorded Beta-2-microglobulin × 1 (P61769) Spike protein S1 × 1 (P0DTC2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;0.1M Imidazole, 20%w/v PEG 6000 Resolution 2.18 Å R-free 0.291

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5SPM2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–274; UniProt 25–298

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 21–119 Not recorded HLA class I heavy chain × 1 (Q5SPM2) Spike protein S1 × 1 (P0DTC2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;0.1M Imidazole, 20%w/v PEG 6000 Resolution 2.18 Å R-free 0.291

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 1–99; UniProt 21–119

Spike protein S1

OrganismNot specified

UniProt P0DTC2

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 361–369 Fragment:Pep16 HLA class I heavy chain × 1 (Q5SPM2) Beta-2-microglobulin × 1 (P61769) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;0.1M Imidazole, 20%w/v PEG 6000 Resolution 2.18 Å R-free 0.291

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.

2152 other PDB entries and 2473 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS2
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–9; UniProt 361–369

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 8xkc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8xkc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8xkc
Deposition date deposition_date2023-12-23
Structure title titleThe structure of HLA-A/Pep16
Keywords keywordsComplex, Peptide presentation, VIRAL PROTEIN/IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM complex; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.29
Radius of gyration Rg (electron density) rg_electron23.11
Forward intensity I(0) i036883100.00
Molecular weight molecular_weight44569.0 kDa
Excluded volume excluded_volume54735 ų
Envelope volume envelope_volume67596 ų
Hydration-shell volume shell_volume24592 ų
Envelope diameter envelope_diameter78.1
Shell Rg shell_rg29.96
Envelope Rg envelope_rg23.11
Shape Rg shape_rg23.08
Total Rg total_rg23.97
Total atoms total_atoms3147
Residues n_residues382
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 dmax75.9
Rg (real space) rg_real24.23
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real3.6880e+07
I(0) uncertainty (real space) i0_real_error4.5440e+05
Rg (reciprocal space) rg_reciprocal24.24
I(0) (reciprocal space) i0_reciprocal36880000.0000
Solution quality estimate total_estimate0.9112
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.1
Skewness Skewness skewness0.245
Kurtosis Kurtosis kurtosis-0.491
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8896000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.950; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)