1AO6
CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN
Summary for 1AO6
Entry DOI | 10.2210/pdb1ao6/pdb |
Descriptor | SERUM ALBUMIN (2 entities in total) |
Functional Keywords | carrier protein, albumin |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P02768 |
Total number of polymer chains | 2 |
Total formula weight | 133142.44 |
Authors | Sugio, S.,Mochizuki, S.,Noda, M.,Kashima, A. (deposition date: 1997-07-18, release date: 1998-05-27, Last modification date: 2024-10-30) |
Primary citation | Sugio, S.,Kashima, A.,Mochizuki, S.,Noda, M.,Kobayashi, K. Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng., 12:439-446, 1999 Cited by PubMed Abstract: A new triclinic crystal form of human serum albumin (HSA), derived either from pool plasma (pHSA) or from a Pichia pastoris expression system (rHSA), was obtained from polyethylene glycol 4000 solution. Three-dimensional structures of pHSA and rHSA were determined at 2.5 A resolution from the new triclinic crystal form by molecular replacement, using atomic coordinates derived from a multiple isomorphous replacement work with a known tetragonal crystal form. The structures of pHSA and rHSA are virtually identical, with an r.m. s. deviation of 0.24 A for all Calpha atoms. The two HSA molecules involved in the asymmetric unit are related by a strict local twofold symmetry such that the Calpha atoms of the two molecules can be superimposed with an r.m.s. deviation of 0.28 A in pHSA. Cys34 is the only cysteine with a free sulfhydryl group which does not participate in a disulfide linkage with any external ligand. Domains II and III both have a pocket formed mostly of hydrophobic and positively charged residues and in which a very wide range of compounds may be accommodated. Three tentative binding sites for long-chain fatty acids, each with different surroundings, are located at the surface of each domain. PubMed: 10388840DOI: 10.1093/protein/12.6.439 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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