1hla

STRUCTURE OF THE HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN, HLA-A2

Method: X-RAY DIFFRACTION Dmax: 72.2 Å Quality: EXCELLENT

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

CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A2) (ALPHA CHAIN)

Homo sapiens

UniProt P01892

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 25–294 Not recorded BETA 2-MICROGLOBULIN × 1 (P61769) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.50 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.

271 other PDB entries and 465 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 1A02_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–270; UniProt 25–294

BETA 2-MICROGLOBULIN

Homo sapiens

UniProt P61769

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain M; UniProt 21–117 Not recorded CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A2) (ALPHA CHAIN) × 1 (P01892) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.50 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.

1313 other PDB entries and 1998 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 1–97; UniProt 21–117

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 1hla

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1hla
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1hla
Deposition date deposition_date1987-10-15
Structure title titleSTRUCTURE OF THE HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN, HLA-A2
Keywords keywordsHISTOCOMPATIBILITY ANTIGEN; HISTOCOMPATIBILITY ANTIGEN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.50
Radius of gyration Rg (electron density) rg_electron22.62
Forward intensity I(0) i031449000.00
Molecular weight molecular_weight42608.0 kDa
Excluded volume excluded_volume51227 ų
Envelope volume envelope_volume37618 ų
Hydration-shell volume shell_volume15544 ų
Envelope diameter envelope_diameter73.3
Shell Rg shell_rg26.41
Envelope Rg envelope_rg21.15
Shape Rg shape_rg22.77
Total Rg total_rg22.94
Total atoms total_atoms
Residues n_residues
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 dmax72.2
Rg (real space) rg_real23.43
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real3.1450e+07
I(0) uncertainty (real space) i0_real_error3.5230e+05
Rg (reciprocal space) rg_reciprocal23.45
I(0) (reciprocal space) i0_reciprocal31450000.0000
Solution quality estimate total_estimate0.9111
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.0
Skewness Skewness skewness0.223
Kurtosis Kurtosis kurtosis-0.455
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha3714000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.962; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1hlaa1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd1hlaa2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.19 — MHC antigen-recognition domain
Superfamily Superfamily superfamilyd.19.1 — MHC antigen-recognition domain
Family Family familyd.19.1.1 — MHC antigen-recognition domain
Domain ID domain_idd1hlam_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)

8. Citations (3)

9. Files and Curves (10)