8vsj

Engineered peptide-specific binder in complex with HLA-DR1/CLIP

Method: ELECTRON MICROSCOPY Dmax: 98.3 Å Quality: GOOD

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

HLA class II histocompatibility antigen, DR alpha chain

Homo sapiens

UniProt P01903

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 26–207 Not recorded HLA class II histocompatibility antigen DR beta chain × 1 (D7RIG0) Superantigen × 1 (Q48898) c44H10 Fab heavy chain × 1 c44H10 Fab light chain × 1 Class-II-associated invariant chain peptide × 1 (P04233) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

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.

139 other PDB entries and 219 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DRA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–182; UniProt 26–207

HLA class II histocompatibility antigen DR beta chain

Homo sapiens

UniProt D7RIG0

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 30–219 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) Superantigen × 1 (Q48898) c44H10 Fab heavy chain × 1 c44H10 Fab light chain × 1 Class-II-associated invariant chain peptide × 1 (P04233) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

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.

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

View Construct and Data Evidence
UniProt name D7RIG0_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–190; UniProt 30–219

Superantigen

Metamycoplasma arthritidis

UniProt Q48898

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 26–149 Mutation:V30C, Q37S, K38I, H39Y, F40L, V41A, Y59D, L72K, L75E, G86D, V88I, D90K, N92G, G93D, delta 94-97, I100V, T110I, I127T, S144C HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) HLA class II histocompatibility antigen DR beta chain × 1 (D7RIG0) c44H10 Fab heavy chain × 1 c44H10 Fab light chain × 1 Class-II-associated invariant chain peptide × 1 (P04233) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

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.

4 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q48898_METAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–120; UniProt 26–149

Class-II-associated invariant chain peptide

Homo sapiens

UniProt P04233

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain P; UniProt 103–117 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) HLA class II histocompatibility antigen DR beta chain × 1 (D7RIG0) Superantigen × 1 (Q48898) c44H10 Fab heavy chain × 1 c44H10 Fab light chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HG2A_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain P; PDBConstruct 1–15; UniProt 103–117

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 8vsj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vsj
Deposition date deposition_date2024-01-24
Structure title titleEngineered peptide-specific binder in complex with HLA-DR1/CLIP
Keywords keywordscomplex, engineered protein, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.70
Radius of gyration Rg (electron density) rg_electron28.83
Forward intensity I(0) i0109615000.00
Molecular weight molecular_weight82752.0 kDa
Excluded volume excluded_volume103550 ų
Envelope volume envelope_volume131580 ų
Hydration-shell volume shell_volume37859 ų
Envelope diameter envelope_diameter104.8
Shell Rg shell_rg36.17
Envelope Rg envelope_rg28.98
Shape Rg shape_rg28.78
Total Rg total_rg29.68
Total atoms total_atoms5832
Residues n_residues711
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 dmax98.3
Rg (real space) rg_real29.63
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.0960e+08
I(0) uncertainty (real space) i0_real_error1.6100e+06
Rg (reciprocal space) rg_reciprocal29.66
I(0) (reciprocal space) i0_reciprocal109600000.0000
Solution quality estimate total_estimate0.8912
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.1
Skewness Skewness skewness0.266
Kurtosis Kurtosis kurtosis-0.346
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20390000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.868; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)