Aspartyl/Asparaginyl beta-hydroxylase (AspH) in complex with Fe, 2-oxoglutarate, succinate and the hydroxylated product of Factor X derived peptide fragment, 12 h O2 exposure
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Aspartyl/Asparaginyl beta-hydroxylase (AspH) in complex with Fe, 2-oxoglutarate, succinate and the hydroxylated product of Factor X derived peptide fragment, 12 h O2 exposure Descriptor: Aspartyl/asparaginyl beta-hydroxylase, FE (III) ION, Factor X light chain, ... Authors: de Munnik, M, Brasnett, A, Rabe, P, Brewitz, L, Park, J, Schofield, C.J, Zhou, T. Deposit date: 2024-12-11 Release date: 2025-12-24 Last modified: 2026-03-11 Method: X-RAY DIFFRACTION (2.14 Å) Cite: Structural basis of the promiscuity of the unusual Fe(II) and 2-oxoglutarate dependent human aspartate/asparagine-beta-hydroxylase. Nat Commun, 2026
天冬氨酰/天冬酰胺基β-羟化酶(aspartyl/asparaginyl beta-hydroxylase, AspH)与铁、2-氧戊二酸、琥珀酸以及因子X衍生肽片段的羟化产物形成复合物,经12小时氧气暴露处理。描述项:天冬氨酰/天冬酰胺基β-羟化酶、三价铁离子、因子X轻链……作者:德·穆尼克(M. de Munnik)、布拉斯内特(A. Brasnett)、拉贝(P. Rabe)、布罗维茨(L. Brewitz)、朴(J. Park)、斯科菲尔德(C.J. Schofield)、周(T. Zhou)。存入日期:2024-12-11,发布日期:2025-12-24,最后修改日期:2026-03-11。实验方法:X射线衍射(2.14埃)。引用文献:非常规铁(II)依赖与2-氧戊二酸依赖型人源天冬氨酸/天冬酰胺-β-羟化酶的催化混杂结构基础,《自然·通讯》(Nat Commun),2026年
创建时间:
2024-12-11



