2qri

Crystal structure of a single chain trimer composed of the MHC I heavy chain H-2Kb WT, beta-2microglobulin, and ovalbumin-derived peptide.

Method: X-RAY DIFFRACTION Dmax: 104.9 Å Quality: EXCELLENT

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

H-2 class I histocompatibility antigen K-B alpha chain, Beta-2 microglobulin, ovalbumin-derived peptide

Mus musculus

UniProt P01901

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 22–301 Fragment:;Fusion protein of ovalbumin-derived peptide, linker, Beta-2 microglobulin, linker, and H-2 class I histocompatibility antigen K-B alpha chain extracellular domain ; No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;298 K;13% PEG 10000, 100 mM MES, pH 6.2, vapor diffusion, hanging drop, temperature 298K Resolution 2.00 Å R-free 0.253
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 22–301 Fragment:;Fusion protein of ovalbumin-derived peptide, linker, Beta-2 microglobulin, linker, and H-2 class I histocompatibility antigen K-B alpha chain extracellular domain ; No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;298 K;13% PEG 10000, 100 mM MES, pH 6.2, vapor diffusion, hanging drop, temperature 298K Resolution 2.00 Å R-free 0.253

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.

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

View Construct and Data Evidence
UniProt name HA1B_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 143–422; UniProt 22–301 Author chain B; PDBConstruct 143–422; UniProt 22–301

H-2 class I histocompatibility antigen K-B alpha chain, Beta-2 microglobulin, ovalbumin-derived peptide

Mus musculus

UniProt Q91XJ8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 21–119 Fragment:;Fusion protein of ovalbumin-derived peptide, linker, Beta-2 microglobulin, linker, and H-2 class I histocompatibility antigen K-B alpha chain extracellular domain ; No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;298 K;13% PEG 10000, 100 mM MES, pH 6.2, vapor diffusion, hanging drop, temperature 298K Resolution 2.00 Å R-free 0.253
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 21–119 Fragment:;Fusion protein of ovalbumin-derived peptide, linker, Beta-2 microglobulin, linker, and H-2 class I histocompatibility antigen K-B alpha chain extracellular domain ; No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;298 K;13% PEG 10000, 100 mM MES, pH 6.2, vapor diffusion, hanging drop, temperature 298K Resolution 2.00 Å R-free 0.253

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.

25 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q91XJ8_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–122; UniProt 21–119 Author chain B; PDBConstruct 24–122; UniProt 21–119

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 2qri

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2qri
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2qri
Deposition date deposition_date2007-07-28
Structure title titleCrystal structure of a single chain trimer composed of the MHC I heavy chain H-2Kb WT, beta-2microglobulin, and ovalbumin-derived peptide.
Keywords keywordsMHC-I, Ova, Single Chain MHC-I, Glycoprotein, Immune response, Membrane, MHC I, Transmembrane, 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_guinier33.82
Radius of gyration Rg (electron density) rg_electron33.09
Forward intensity I(0) i0136000000.00
Molecular weight molecular_weight90680.0 kDa
Excluded volume excluded_volume112450 ų
Envelope volume envelope_volume155280 ų
Hydration-shell volume shell_volume39127 ų
Envelope diameter envelope_diameter110.6
Shell Rg shell_rg40.16
Envelope Rg envelope_rg31.96
Shape Rg shape_rg33.07
Total Rg total_rg33.71
Total atoms total_atoms6396
Residues n_residues796
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 dmax104.9
Rg (real space) rg_real33.71
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.3600e+08
I(0) uncertainty (real space) i0_real_error2.3290e+06
Rg (reciprocal space) rg_reciprocal33.78
I(0) (reciprocal space) i0_reciprocal136000000.0000
Solution quality estimate total_estimate0.9122
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.6
Skewness Skewness skewness0.105
Kurtosis Kurtosis kurtosis-0.658
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14160000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.970; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.946

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id2qriA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2qriA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily10 — MHC class I-like antigen recognition-like
Domain ID domain_id2qriA03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2qriB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2qriB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily10 — MHC class I-like antigen recognition-like
Domain ID domain_id2qriB03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)