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1AO6

CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN

Summary for 1AO6
Entry DOI10.2210/pdb1ao6/pdb
DescriptorSERUM ALBUMIN (2 entities in total)
Functional Keywordscarrier protein, albumin
Biological sourceHomo sapiens (human)
Cellular locationSecreted: P02768
Total number of polymer chains2
Total formula weight133142.44
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 citationSugio, 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: 10388840
DOI: 10.1093/protein/12.6.439
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

237735

数据于2025-06-18公开中

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