5vcl

Structure of the Qdm peptide bound to Qa-1a

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

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

H2-T23 protein

Mus musculus

UniProt Q31153

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 21–297 Fragment:UNP residues 21-297 Beta-2-microglobulin × 1 (P01887) Qdm peptide × 1 (P01897) GOL GLYCEROL × 4 NA SODIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;295 K;5% polyethylene glycol 1000, 40% ethylene glycol, 100 mM HEPES pH 6.5 Resolution 2.05 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 Q31153_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–278; UniProt 21–297

Beta-2-microglobulin

Mus musculus

UniProt P01887

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 H2-T23 protein × 1 (Q31153) Qdm peptide × 1 (P01897) GOL GLYCEROL × 4 NA SODIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;295 K;5% polyethylene glycol 1000, 40% ethylene glycol, 100 mM HEPES pH 6.5 Resolution 2.05 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.

290 other PDB entries and 483 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–99; UniProt 21–119

Qdm peptide

OrganismNot specified

UniProt P01897

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 P; UniProt 3–11 Fragment:UNP residues 3-11 H2-T23 protein × 1 (Q31153) Beta-2-microglobulin × 1 (P01887) GOL GLYCEROL × 4 NA SODIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;295 K;5% polyethylene glycol 1000, 40% ethylene glycol, 100 mM HEPES pH 6.5 Resolution 2.05 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.

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

View Construct and Data Evidence
UniProt name HA1L_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–9; UniProt 3–11

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 5vcl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5vcl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5vcl
Deposition date deposition_date2017-03-31
Structure title titleStructure of the Qdm peptide bound to Qa-1a
Keywords keywordsantigen-presentation, immune system, MHC; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.05
Radius of gyration Rg (electron density) rg_electron23.12
Forward intensity I(0) i035809300.00
Molecular weight molecular_weight45334.0 kDa
Excluded volume excluded_volume56286 ų
Envelope volume envelope_volume68259 ų
Hydration-shell volume shell_volume24714 ų
Envelope diameter envelope_diameter79.1
Shell Rg shell_rg29.97
Envelope Rg envelope_rg23.27
Shape Rg shape_rg23.13
Total Rg total_rg23.93
Total atoms total_atoms3189
Residues n_residues385
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_real24.00
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real3.5810e+07
I(0) uncertainty (real space) i0_real_error4.9320e+05
Rg (reciprocal space) rg_reciprocal24.01
I(0) (reciprocal space) i0_reciprocal35810000.0000
Solution quality estimate total_estimate0.9075
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.4
Skewness Skewness skewness0.279
Kurtosis Kurtosis kurtosis-0.429
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8829000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id5vclA01
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_id5vclA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5vclB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)