1HSA

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

Summary for 1HSA

DescriptorCLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-B*2705), BETA 2-MICROGLOBULIN, MODEL PEPTIDE SEQUENCE - ARAAAAAAA, ... (4 entities in total)
Functional Keywordshistocompatibility antigen
Biological sourceHomo sapiens (human)
Cellular locationMembrane; Single-pass type I membrane protein P03989
Secreted P61769
Total number of polymer chains6
Total molecular weight88840.3
Authors
Madden, D.R.,Gorga, J.C.,Strominger, J.L.,Wiley, D.C. (deposition date: 1992-08-11, release date: 1992-10-15, Last modification date: 2011-07-13)
Primary citation
Madden, D.R.,Gorga, J.C.,Strominger, J.L.,Wiley, D.C.
The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC.
Cell(Cambridge,Mass.), 70:1035-1048, 1992
PubMed: 1525820 (PDB entries with the same primary citation)
DOI: 10.1016/0092-8674(92)90252-8
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.1 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers402.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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PDB entries from 2020-08-05