1S4C
YHCH PROTEIN (HI0227) COPPER COMPLEX
1S4C の概要
エントリーDOI | 10.2210/pdb1s4c/pdb |
関連するPDBエントリー | 1JOP |
分子名称 | Protein HI0227, COPPER (II) ION, ACETATE ION, ... (4 entities in total) |
機能のキーワード | double-stranded beta-helix, structural genomics, unknown function |
由来する生物種 | Haemophilus influenzae |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 71078.48 |
構造登録者 | Teplyakov, A.,Obmolova, G.,Toedt, J.,Gilliland, G.L. (登録日: 2004-01-15, 公開日: 2005-06-14, 最終更新日: 2023-08-23) |
主引用文献 | Teplyakov, A.,Obmolova, G.,Toedt, J.,Galperin, M.Y.,Gilliland, G.L. Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism. J.Bacteriol., 187:5520-5527, 2005 Cited by PubMed Abstract: The yhcH gene is part of the nan operon in bacteria that encodes proteins involved in sialic acid catabolism. Determination of the crystal structure of YhcH from Haemophilus influenzae was undertaken as part of a structural genomics effort in order to assist with the functional assignment of the protein. The structure was determined at 2.2-A resolution by multiple-wavelength anomalous diffraction. The protein fold is a variation of the double-stranded beta-helix. Two antiparallel beta-sheets form a funnel opened at one side, where a putative active site contains a copper ion coordinated to the side chains of two histidine and two carboxylic acid residues. A comparison to other proteins with a similar fold and analysis of the genomic context suggested that YhcH may be a sugar isomerase involved in processing of exogenous sialic acid. PubMed: 16077096DOI: 10.1128/JB.187.16.5520-5527.2005 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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