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1NST

THE SULFOTRANSFERASE DOMAIN OF HUMAN HAPARIN SULFATE N-DEACETYLASE/N-SULFOTRANSFERASE

1NST の概要
エントリーDOI10.2210/pdb1nst/pdb
分子名称HEPARAN SULFATE N-DEACETYLASE/N-SULFOTRANSFERASE, ADENOSINE-3'-5'-DIPHOSPHATE (3 entities in total)
機能のキーワードsulfotransferase, pap, haparin sulfate, haparin sulfate biosynthesis, glycoprotein
由来する生物種Homo sapiens (human)
タンパク質・核酸の鎖数1
化学式量合計38344.45
構造登録者
Kakuta, Y.,Pedersen, L.C.,Negishi, M. (登録日: 1998-09-07, 公開日: 1999-09-16, 最終更新日: 2024-10-16)
主引用文献Kakuta, Y.,Sueyoshi, T.,Negishi, M.,Pedersen, L.C.
Crystal structure of the sulfotransferase domain of human heparan sulfate N-deacetylase/ N-sulfotransferase 1.
J.Biol.Chem., 274:10673-10676, 1999
Cited by
PubMed Abstract: Heparan sulfate N-deacetylase/N-sulfotransferase (HSNST) catalyzes the first and obligatory step in the biosynthesis of heparan sulfates and heparin. The crystal structure of the sulfotransferase domain (NST1) of human HSNST-1 has been determined at 2.3-A resolution in a binary complex with 3'-phosphoadenosine 5'-phosphate (PAP). NST1 is approximately spherical with an open cleft, and consists of a single alpha/beta fold with a central five-stranded parallel beta-sheet and a three-stranded anti-parallel beta-sheet bearing an interstrand disulfide bond. The structural regions alpha1, alpha6, beta1, beta7, 5'-phosphosulfate binding loop (between beta1 and alpha1), and a random coil (between beta8 and alpha13) constitute the PAP binding site of NST1. The alpha6 and random coil (between beta2 and alpha2), which form an open cleft near the 5'-phosphate of the PAP molecule, may provide interactions for substrate binding. The conserved residue Lys-614 is in position to form a hydrogen bond with the bridge oxygen of the 5'-phosphate.
PubMed: 10196134
DOI: 10.1074/jbc.274.16.10673
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.3 Å)
構造検証レポート
Validation report summary of 1nst
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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