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2Z6P

Crystal Structure of the Ufc1, Ufm1 conjugating enzyme 1

Summary for 2Z6P
Entry DOI10.2210/pdb2z6p/pdb
Related2Z6O
DescriptorUfm1-conjugating enzyme 1 (2 entities in total)
Functional Keywordsufc1, ufm1, ubiquitin, ubl, polymorphism, ubl conjugation pathway, ligase
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight20038.54
Authors
Mizushima , T.,Tatsumi, K.,Ozaki, Y.,Kawakami, T.,Suzuki, A.,Ogasahara, K.,Komatsu, M.,Kominami, E.,Tanaka, K.,Yamane, T. (deposition date: 2007-08-06, release date: 2007-09-25, Last modification date: 2024-11-13)
Primary citationMizushima, T.,Tatsumi, K.,Ozaki, Y.,Kawakami, T.,Suzuki, A.,Ogasahara, K.,Komatsu, M.,Kominami, E.,Tanaka, K.,Yamane, T.
Crystal structure of Ufc1, the Ufm1-conjugating enzyme
Biochem.Biophys.Res.Commun., 362:1079-1084, 2007
Cited by
PubMed Abstract: Ubiquitin and ubiquitin-like protein-conjugating enzymes play central roles in posttranslational modification processes. The ubiquitin-fold modifier 1 (Ufm1), one of a variety of ubiquitin-like modifiers, is covalently attached to target proteins via Uba5 and Ufm1-conjugating enzyme 1 (Ufc1), which are analogous to the E1 and E2 ubiquitylation enzymes. As Ufm1-related proteins are conserved in metazoa and plants, the Ufm1 system likely plays important roles in various multicellular organisms. Herein, we report the X-ray structure of human Ufc1 determined at 1.6 A resolution. The Ufc1 structure comprises a canonical E2 domain and an additional N-terminal domain. The Uba5 binding site on Ufc1 was assigned by structural comparison of Ufc1 and Ubc12 and related mutational analyses. In addition, we show that the N-terminal unique domain of Ufc1 contributes to thermal stability.
PubMed: 17825256
DOI: 10.1016/j.bbrc.2007.08.129
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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