9bf9

Human LAG-3-HLA-DR1 complex

Method: X-RAY DIFFRACTION Dmax: 93.3 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 Other combination Heteromer Protein × 8 其他Polymer 2 PDB declaration: tetrameric(4) Count mismatch; review required Chain A; UniProt 30–206 Fragment:UNP residues 30-206 HLA class II histocompatibility antigen DR beta chain × 2 (D7RIG0) Membrane protein × 2 (P0DTC5) Lymphocyte activation gene 3 protein × 2 (P18627) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 SO4 SULFATE ION × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;22% PEG 8000, 0.16M Li2SO4, 0.1M HEPES pH 7.6 Resolution 3.40 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.

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 5–181; UniProt 30–206

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 Other combination Heteromer Protein × 8 其他Polymer 2 PDB declaration: tetrameric(4) Count mismatch; review required Chain B; UniProt 29–227 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 2 (P01903) Membrane protein × 2 (P0DTC5) Lymphocyte activation gene 3 protein × 2 (P18627) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 SO4 SULFATE ION × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;22% PEG 8000, 0.16M Li2SO4, 0.1M HEPES pH 7.6 Resolution 3.40 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.

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 13–211; UniProt 29–227

Membrane protein

Severe acute respiratory syndrome coronavirus 2

UniProt P0DTC5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 8 其他Polymer 2 PDB declaration: tetrameric(4) Count mismatch; review required Chain G; UniProt 177–189 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 2 (P01903) HLA class II histocompatibility antigen DR beta chain × 2 (D7RIG0) Lymphocyte activation gene 3 protein × 2 (P18627) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 SO4 SULFATE ION × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;22% PEG 8000, 0.16M Li2SO4, 0.1M HEPES pH 7.6 Resolution 3.40 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.

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

View Construct and Data Evidence
UniProt name VME1_SARS2
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–13; UniProt 177–189

Lymphocyte activation gene 3 protein

Homo sapiens

UniProt P18627

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 8 其他Polymer 2 PDB declaration: tetrameric(4) Count mismatch; review required Chain D; UniProt 23–429 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 2 (P01903) HLA class II histocompatibility antigen DR beta chain × 2 (D7RIG0) Membrane protein × 2 (P0DTC5) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 SO4 SULFATE ION × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;22% PEG 8000, 0.16M Li2SO4, 0.1M HEPES pH 7.6 Resolution 3.40 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.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LAG3_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 3–409; UniProt 23–429

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 9bf9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bf9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9bf9
Deposition date deposition_date2024-04-17
最后修订 last_revision2024-12-25
Structure title titleHuman LAG-3-HLA-DR1 complex
Keywords keywordsImmune receptor complex Class II Human Leucocyte Antigen Lymphocyte activation Gene-3 IMMUNE SYSTEM, 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_guinier29.86
Radius of gyration Rg (electron density) rg_electron28.84
Forward intensity I(0) i080930700.00
Molecular weight molecular_weight68967.0 kDa
Excluded volume excluded_volume85582 ų
Envelope volume envelope_volume116410 ų
Hydration-shell volume shell_volume33476 ų
Envelope diameter envelope_diameter92.5
Shell Rg shell_rg36.15
Envelope Rg envelope_rg28.62
Shape Rg shape_rg28.83
Total Rg total_rg29.60
Total atoms total_atoms4865
Residues n_residues596
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 dmax93.3
Rg (real space) rg_real29.75
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real8.0930e+07
I(0) uncertainty (real space) i0_real_error1.1110e+06
Rg (reciprocal space) rg_reciprocal29.80
I(0) (reciprocal space) i0_reciprocal80930000.0000
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_primary91.5
Skewness Skewness skewness0.143
Kurtosis Kurtosis kurtosis-0.651
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13770000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.961; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)