1ND7: WW domain-containing protein 1

Name: PDB 1ND7: Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase
Published: 2003-09-23
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

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.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,118
Mol. weight: 44.29 kDa
Released: 23 Sept 2003

Explore 1ND7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 22 helices, 14 β-strands

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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
WW domain-containing protein 1	A	protein	374	Homo sapiens	Q9H0M0 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1ND7_1 WW domain-containing protein 1 (chains A)
HMGFRWKLAHFRYLCQSNALPSHVKINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGE
EGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRF
IAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMY
FSVDMEILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEV
VPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRHYTRNSKQIIWFWQFVKETDNEVR
MRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVGKDTWLPRSHTCFNRLDLPPYKSYE
QLKEKLLFAIEETE

Primary citation

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:

5HPS 2.05 Å, System-wide modulation of HECT E3 ligases with selective ubiquitin variant probes: WWP1…
6J1X 2.3 Å, WWP1 close conformation
8EI4 2.43 Å, Crystal structure of the WWP1 HECT domain in complex with H302, a Helicon Polypeptide
6J1Y 2.55 Å, Semi-open conformation E3 ligase
5HPT 2.84 Å, System-wide modulation of HECT E3 ligases with selective ubiquitin variant probes: WWP1,…
9EQK 3.0 Å, WWP1 WW2-2,3-linker-WW3-WW4-HECT (WWP1-2L34H) with ordered WW2 domain
2OP7 WW4

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