1BM0

CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN

1BM0 の概要

• エントリーDOI: 10.2210/pdb1bm0/pdb
• 分子名称: SERUM ALBUMIN (2 entities in total)
• 機能のキーワード: carrier protein, albumin
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P02768
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 133142.44

構造登録者

Sugio, S.,Kashima, A.,Mochizuki, S.,Noda, M.,Kobayashi, K. (登録日: 1998-07-28, 公開日: 1999-07-28, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)