7mkb

Human leukocyte antigen A*0201 in complex with SARS-CoV-2 epitope YLQPRTFLL

Method: X-RAY DIFFRACTION Dmax: 74.7 Å Quality: EXCELLENT

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

MHC class I antigen

Homo sapiens

UniProt U5YJM1

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 Fragment:UNP residues 25-298 Beta-2-microglobulin × 1 (P61769) Spike protein S1 × 1 (P0DTC2) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;290 K;17% PEG10000, 0.1 M Bis-Tris, pH 5.5, 0.1 M ammonium acetate Resolution 1.90 Å R-free 0.209

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.

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

View Construct and Data Evidence
UniProt name U5YJM1_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 Fragment:UNP residues 21-119 MHC class I antigen × 1 (U5YJM1) Spike protein S1 × 1 (P0DTC2) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;290 K;17% PEG10000, 0.1 M Bis-Tris, pH 5.5, 0.1 M ammonium acetate Resolution 1.90 Å R-free 0.209

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

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 269–277 Fragment:epitope YLQPRTFLL (UNP residues 269-277) MHC class I antigen × 1 (U5YJM1) Beta-2-microglobulin × 1 (P61769) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;290 K;17% PEG10000, 0.1 M Bis-Tris, pH 5.5, 0.1 M ammonium acetate Resolution 1.90 Å R-free 0.209

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 269–277

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 7mkb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mkb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7mkb
Deposition date deposition_date2021-04-22
Structure title titleHuman leukocyte antigen A*0201 in complex with SARS-CoV-2 epitope YLQPRTFLL
Keywords keywords;SARS-CoV-2, CD8+, epitope, HLA, human major histocompatibility complex, MHC-I, YLQPRTFLL, HLA-A2, HLA-A*02:01 IMMUNE SYSTEM-VIRAL PROTEIN complex, IMMUNE SYSTEM-VIRAL PROTEIN complex ;; IMMUNE SYSTEM/VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.08
Radius of gyration Rg (electron density) rg_electron22.90
Forward intensity I(0) i036426200.00
Molecular weight molecular_weight44891.0 kDa
Excluded volume excluded_volume55417 ų
Envelope volume envelope_volume67867 ų
Hydration-shell volume shell_volume24764 ų
Envelope diameter envelope_diameter78.3
Shell Rg shell_rg29.85
Envelope Rg envelope_rg22.99
Shape Rg shape_rg22.88
Total Rg total_rg23.79
Total atoms total_atoms3170
Residues n_residues383
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 dmax74.7
Rg (real space) rg_real24.01
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real3.6430e+07
I(0) uncertainty (real space) i0_real_error4.3820e+05
Rg (reciprocal space) rg_reciprocal24.03
I(0) (reciprocal space) i0_reciprocal36430000.0000
Solution quality estimate total_estimate0.9097
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.3
Skewness Skewness skewness0.242
Kurtosis Kurtosis kurtosis-0.476
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9662000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)