4OYK: HOIP PUB domain

Structure of HOIP PUB domain bound to OTULIN PIM. Determined by X-ray diffraction at 2.0 Å resolution. Released 21 May 2014.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,262
Mol. weight: 44.96 kDa
Released: 21 May 2014

Explore 4OYK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4OYK contains 26 α-helices and 6 β-strands across 4 chains. 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: 13 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	10-23	14
α-helix	31-38	8
α-helix	44-47	4
α-helix	53-58	6
α-helix	65-87	23
α-helix	91-92	2
β-strand	97-99	3	1
α-helix	103-104	2
α-helix	105-109	5
α-helix	115-122	8
β-strand	126-128	3	1
β-strand	131-133	3	1
α-helix	134-135	2
α-helix	143-165	23
α-helix	171-174	4
α-helix	175-177	3

Chain B: 11 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	7-23	17
α-helix	35-39	5
α-helix	44-47	4
α-helix	53-58	6
α-helix	65-87	23
α-helix	91-92	2
β-strand	97-99	3	2
α-helix	103-107	5
α-helix	109-111	3
α-helix	115-122	8
β-strand	126-128	3	2
β-strand	131-133	3	2
α-helix	143-164	22
α-helix	171-177	7

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	59-63	5

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	59-66	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase RNF31	A, B	protein	177	Homo sapiens	Q96EP0 (AlphaFold model)
Ubiquitin thioesterase otulin	C, D	protein	19	Homo sapiens	Q96BN8 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4OYK_1 E3 ubiquitin-protein ligase RNF31 (chains A, B)
GPEEERAFLVAREELASALRRDSGQAFSLEQLRPLLASSLPLAARYLQLDAARLVRCNAH
GEPRNYLNTLSTALNILEKYGRNLLSPQRPRYWRGVKFNNPVFRSTVDAVQGGRDVLRLY
GYTEEQPDGLSFPEGQEEPDEHQVATVTLEVLLLRTELSLLLQNTHPRQQALEQLLE

Sequence of entity 2 (C, D), FASTA

>4OYK_2 Ubiquitin thioesterase otulin (chains C, D)
AEHEEDMYRAADEIEKEKE

Primary citation

Molecular Basis and Regulation of OTULIN-LUBAC Interaction. Elliott, P.R., Nielsen, S.V., Marco-Casanova, P. et al. Mol Cell (2014) 54:335-348. DOI 10.1016/j.molcel.2014.03.018 · PubMed

Other PDB entries of the same protein (UniProt Q96EP0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6KC5 1.54 Å, HOIP-HOIPIN1 complex
4LJO 1.56 Å, Structure of an active ligase (HOIP)/ubiquitin transfer complex
7V8F 1.66 Å, Crystal structure of UBE2L3 bound to HOIP RING1 domain.
4P09 1.7 Å, Crystal structure of HOIP PUB domain
9B0B 1.7 Å, Structure of Optineurin bound to HOIP NZF1 domain
9B12 1.81 Å, Structure of Optineurin bound to HOIP NZF1 domain and M1-linked diubiquitin, crystal…
4OWF 2.0 Å, Crystal structure of the NEMO CoZi in complex with HOIP NZF1 domain
6SC5 2.1 Å, dAb3/HOIP-RBR-Ligand2
6SC8 2.11 Å, dAb3/HOIP-RBR-Ligand4
6KC6 2.12 Å, HOIP-HOIPIN8 complex
4LJP 2.15 Å, Structure of an active ligase (HOIP-H889A)/ubiquitin transfer complex
6GZY 2.15 Å, HOIP-fragment5 complex

Browse structure collections

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