PDBe 1hsa

X-ray diffraction
2.1Å resolution

THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
HLA class I histocompatibility antigen, B-27 alpha chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 276 amino acids
Theoretical weight: 31.93 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: NEW P03989 (Residues: 25-300; Coverage: 82%)
Gene names: HLA-B, HLAB
Sequence domains:
Structure domains:
Beta-2-microglobulin Chains: B, E
Molecule details ›
Chains: B, E
Length: 99 amino acids
Theoretical weight: 11.75 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: NEW P61769 (Residues: 21-119; Coverage: 100%)
Gene names: B2M, CDABP0092, HDCMA22P
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
MODEL PEPTIDE SEQUENCE - ARAAAAAAA Chains: C, F
Molecule details ›
Chains: C, F
Length: 9 amino acids
Theoretical weight: 744 Da

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 45.1Å b: 69.8Å c: 81.1Å
α: 80.3° β: 88.6° γ: 89.9°
R-values:
R R work R free
0.203 0.203 not available
Expression system: Not provided