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

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)