6J1X: WWP1 close conformation

Name: PDB 6J1X: WWP1 close conformation
Published: 2019-07-24
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

WWP1 close conformation. Determined by X-ray diffraction at 2.3 Å resolution. Released 24 Jul 2019.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,710
Mol. weight: 65.26 kDa
Released: 24 Jul 2019

Explore 6J1X in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6J1X contains 28 α-helices and 22 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 B: 28 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	387-391	5	1
β-strand	397-401	5	1
β-strand	407-408	2	1
α-helix	411-412	2
α-helix	414-423	10
α-helix	434-443	10
α-helix	497-499	3
β-strand	502-506	5	2
β-strand	512-516	5	2
β-strand	521-523	3	2
β-strand	525	1	3
β-strand	532	1	3
α-helix	540-543	4
α-helix	547-560	14
β-strand	566-571	6	4
α-helix	573-575	3
α-helix	576-581	6
α-helix	589-593	5
β-strand	595-600	6	4
α-helix	610-622	13
α-helix	626-628	3
β-strand	631-635	5	5
β-strand	639-643	5	5
α-helix	645-649	5
α-helix	653-669	17
α-helix	680-686	7
α-helix	689-691	3
α-helix	693-699	7
α-helix	701-712	12
β-strand	723	1	6
β-strand	725-730	6	7
β-strand	733-738	6	7
α-helix	743-745	3
β-strand	747	1	6
α-helix	753-766	14
α-helix	770-781	12
α-helix	786-789	4
α-helix	794-802	9
α-helix	809-814	6
β-strand	817-819	3	8
α-helix	826-837	12
α-helix	840-851	12
α-helix	861-863	3
β-strand	865-866	2	9
β-strand	869-870	2	9
β-strand	874-877	4	8
β-strand	886-888	3	8
α-helix	889-891	3
β-strand	893-896	4	8
α-helix	902-914	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
NEDD4-like E3 ubiquitin-protein ligase WWP1	B	protein	550	Homo sapiens	Q9H0M0 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>6J1X_1 NEDD4-like E3 ubiquitin-protein ligase WWP1 (chains B)
GPGSEFRPQPLPPGWERRVDDRRRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQG
AMQQFNQRYLYSASMLAAENDPYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL
QNEEPLPEGWEIRYTREGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERGFRWKLA
HFRYLCQSNALPSHVKINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLA
REWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMALFHGK
FIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILG
KVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYF
DEKELEVMLCGMQEVDLADWQRNTVYRHYTRNSKQIIWFWQFVKETDNEVRMRLLQFVTG
TCRLPLGGFAELMGSNGPQKFCIEKVGKDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFA
IEETEGFGQE

Primary citation

A multi-lock inhibitory mechanism for fine-tuning enzyme activities of the HECT family E3 ligases. Wang, Z., Liu, Z., Chen, X. et al. Nat Commun (2019) 10:3162-3162. DOI 10.1038/s41467-019-11224-7 · 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…
1ND7 2.1 Å, Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain…
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

Browse structure collections

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