Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase. Determined by X-ray diffraction at 2.1 Å resolution. Released 23 Sept 2003.
Explore 1ND7 in 3D Show helices and sheets RCSB PDB PDBe
1ND7 contains 22 α-helices and 14 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 547-560 | 14 | |
| β-strand | 566-571 | 6 | 1 |
| α-helix | 576-585 | 10 | |
| α-helix | 589-593 | 5 | |
| β-strand | 595-600 | 6 | 1 |
| α-helix | 610-623 | 14 | |
| α-helix | 626-628 | 3 | |
| β-strand | 631-633 | 3 | 2 |
| β-strand | 641-643 | 3 | 2 |
| α-helix | 645-649 | 5 | |
| α-helix | 653-669 | 17 | |
| α-helix | 680-686 | 7 | |
| α-helix | 693-697 | 5 | |
| α-helix | 701-711 | 11 | |
| β-strand | 723 | 1 | 3 |
| β-strand | 725-726 | 2 | 4 |
| β-strand | 737-738 | 2 | 4 |
| α-helix | 743-745 | 3 | |
| β-strand | 747 | 1 | 3 |
| α-helix | 753-766 | 14 | |
| α-helix | 770-783 | 14 | |
| α-helix | 786-789 | 4 | |
| α-helix | 794-802 | 9 | |
| α-helix | 809-814 | 6 | |
| β-strand | 816-819 | 4 | 5 |
| α-helix | 826-837 | 12 | |
| α-helix | 840-851 | 12 | |
| α-helix | 861-863 | 3 | |
| β-strand | 865-866 | 2 | 6 |
| β-strand | 869-870 | 2 | 6 |
| β-strand | 873-876 | 4 | 5 |
| α-helix | 884-885 | 2 | |
| β-strand | 886-888 | 3 | 5 |
| α-helix | 889-891 | 3 | |
| β-strand | 893-895 | 3 | 5 |
| α-helix | 902-914 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| WW domain-containing protein 1 | A | protein | 374 | Homo sapiens | Q9H0M0 (AlphaFold model) |
>1ND7_1 WW domain-containing protein 1 (chains A) HMGFRWKLAHFRYLCQSNALPSHVKINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGE EGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRF IAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMY FSVDMEILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEV VPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRHYTRNSKQIIWFWQFVKETDNEVR MRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVGKDTWLPRSHTCFNRLDLPPYKSYE QLKEKLLFAIEETE
Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase. Verdecia, M.A., Joaziero, C.A.P., Wells, N.J. et al. Mol Cell (2003) 11:249-259. DOI 10.1016/S1097-2765(02)00774-8 · PubMed
Other PDB entries of the same protein (UniProt Q9H0M0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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