8euq

Crystal structure of HLA-DRA*01:01/HLA-DRB1*04:01 in complex with c44H10 Fab

Method: X-RAY DIFFRACTION Dmax: 123.2 Å Quality: EXCELLENT

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 Insufficient information Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 28–206 Not recorded c44H10 Fab light chain × 1 Hemagglutinin HA1 chain,HLA class II histocompatibility antigen DR beta chain × 1 (P04664,A0A1V1IGJ9) c44H10 Fab heavy chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;1.7 M ammonium sulfate, 15% glycerol, 0.085 M HEPES, 1.7% PEG400, with crystal seeds previously grown in 2 M ammonium sulfate, 0.1 M bis-tris pH 5.5 Resolution 3.09 Å R-free 0.244
2 Insufficient information Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 28–206 Not recorded c44H10 Fab light chain × 1 Hemagglutinin HA1 chain,HLA class II histocompatibility antigen DR beta chain × 1 (P04664,A0A1V1IGJ9) c44H10 Fab heavy chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;1.7 M ammonium sulfate, 15% glycerol, 0.085 M HEPES, 1.7% PEG400, with crystal seeds previously grown in 2 M ammonium sulfate, 0.1 M bis-tris pH 5.5 Resolution 3.09 Å R-free 0.244

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 218 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 1–179; UniProt 28–206 Author chain F; PDBConstruct 1–179; UniProt 28–206

Hemagglutinin HA1 chain,HLA class II histocompatibility antigen DR beta chain

Homo sapiens

UniProt A0A1V1IGJ9

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 Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 30–219 Mutation:A3G, C4A in the hemagglutinin peptide that was used HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) c44H10 Fab light chain × 1 c44H10 Fab heavy chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;1.7 M ammonium sulfate, 15% glycerol, 0.085 M HEPES, 1.7% PEG400, with crystal seeds previously grown in 2 M ammonium sulfate, 0.1 M bis-tris pH 5.5 Resolution 3.09 Å R-free 0.244
2 Insufficient information Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 30–219 Mutation:A3G, C4A in the hemagglutinin peptide that was used HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) c44H10 Fab light chain × 1 c44H10 Fab heavy chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;1.7 M ammonium sulfate, 15% glycerol, 0.085 M HEPES, 1.7% PEG400, with crystal seeds previously grown in 2 M ammonium sulfate, 0.1 M bis-tris pH 5.5 Resolution 3.09 Å R-free 0.244

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A1V1IGJ9_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 28–217; UniProt 30–219 Author chain G; PDBConstruct 28–217; UniProt 30–219

Hemagglutinin HA1 chain,HLA class II histocompatibility antigen DR beta chain

Homo sapiens

UniProt P04664

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 Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 304–318 Mutation:A3G, C4A in the hemagglutinin peptide that was used HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) c44H10 Fab light chain × 1 c44H10 Fab heavy chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;1.7 M ammonium sulfate, 15% glycerol, 0.085 M HEPES, 1.7% PEG400, with crystal seeds previously grown in 2 M ammonium sulfate, 0.1 M bis-tris pH 5.5 Resolution 3.09 Å R-free 0.244
2 Insufficient information Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 304–318 Mutation:A3G, C4A in the hemagglutinin peptide that was used HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) c44H10 Fab light chain × 1 c44H10 Fab heavy chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;1.7 M ammonium sulfate, 15% glycerol, 0.085 M HEPES, 1.7% PEG400, with crystal seeds previously grown in 2 M ammonium sulfate, 0.1 M bis-tris pH 5.5 Resolution 3.09 Å R-free 0.244

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HEMA_I69A0
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–15; UniProt 304–318 Author chain G; PDBConstruct 1–15; UniProt 304–318

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 8euq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8euq
Deposition date deposition_date2022-10-19
Structure title titleCrystal structure of HLA-DRA*01:01/HLA-DRB1*04:01 in complex with c44H10 Fab
Keywords keywordsMHC class II, HLA-DR, Antibody, 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_guinier41.08
Radius of gyration Rg (electron density) rg_electron40.40
Forward intensity I(0) i0532436000.00
Molecular weight molecular_weight185400.0 kDa
Excluded volume excluded_volume230290 ų
Envelope volume envelope_volume329130 ų
Hydration-shell volume shell_volume66334 ų
Envelope diameter envelope_diameter122.1
Shell Rg shell_rg48.30
Envelope Rg envelope_rg38.34
Shape Rg shape_rg40.40
Total Rg total_rg40.85
Total atoms total_atoms13053
Residues n_residues1631
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 dmax123.2
Rg (real space) rg_real40.83
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real5.3240e+08
I(0) uncertainty (real space) i0_real_error8.5680e+06
Rg (reciprocal space) rg_reciprocal41.08
I(0) (reciprocal space) i0_reciprocal532600000.0000
Solution quality estimate total_estimate0.9033
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.6
Skewness Skewness skewness-0.056
Kurtosis Kurtosis kurtosis-0.704
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha66220000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id8euqC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8euqC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8euqD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8euqD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8euqH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8euqH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8euqI01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8euqI02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)