1UOR
X-RAY STUDY OF RECOMBINANT HUMAN SERUM ALBUMIN. PHASES DETERMINED BY MOLECULAR REPLACEMENT METHOD, USING LOW RESOLUTION STRUCTURE MODEL OF TETRAGONAL FORM OF HUMAN SERUM ALBUMIN
Summary for 1UOR
Entry DOI | 10.2210/pdb1uor/pdb |
Descriptor | SERUM ALBUMIN (1 entity in total) |
Functional Keywords | plasma protein, metal-binding protein, metal binding protein |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P02768 |
Total number of polymer chains | 1 |
Total formula weight | 66571.22 |
Authors | Carter, D.C.,Ho, J.X. (deposition date: 1998-03-10, release date: 1998-05-27, Last modification date: 2024-11-20) |
Primary citation | He, X.M.,Carter, D.C. Atomic structure and chemistry of human serum albumin. Nature, 358:209-215, 1992 Cited by PubMed Abstract: The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 A. It comprises three homologous domains that assemble to form a heart-shaped molecule. Each domain is a product of two subdomains that possess common structural motifs. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. The structure explains numerous physical phenomena and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serum albumin. PubMed: 1630489DOI: 10.1038/358209a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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