7UYJ: RNF31

Structure of RNF31 in complex with FP06652, a Helicon Polypeptide. Determined by X-ray diffraction at 2.32 Å resolution. Released 28 Dec 2022.

Method: X-ray diffraction
Resolution: 2.32 Å
Organisms: Homo sapiens, synthetic construct
Chains: 4
Atoms: 3,072
Mol. weight: 45.76 kDa
Ligands: WHL, NH2
Released: 28 Dec 2022

Explore 7UYJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7UYJ contains 21 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: 10 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	4-23	20
α-helix	31-38	8
α-helix	44-47	4
α-helix	53-58	6
α-helix	65-87	23
β-strand	97-99	3	1
α-helix	103-107	5
α-helix	109-111	3
α-helix	115-122	8
β-strand	126-127	2	1
β-strand	131-133	3	1
α-helix	143-164	22
α-helix	171-174	4

Chain B: 9 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	4-23	20
α-helix	31-38	8
α-helix	53-58	6
α-helix	65-86	22
β-strand	97-98	2	2
α-helix	103-106	4
α-helix	109-111	3
α-helix	115-122	8
β-strand	126-127	2	2
β-strand	132-133	2	2
α-helix	134-135	2
α-helix	143-164	22

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-15	13

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-15	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase RNF31	A, B	protein	184	Homo sapiens	Q96EP0 (AlphaFold model)
Helicon FP06652	C, D	protein	17	synthetic construct

Sequence of entity 1 (A, B), FASTA

>7UYJ_1 E3 ubiquitin-protein ligase RNF31 (chains A, B)
GPLGSMPGEEEERAFLVAREELASALRRDSGQAFSLEQLRPLLASSLPLAARYLQLDAAR
LVRCNAHGEPRNYLNTLSTALNILEKYGRNLLSPQRPRYWRGVKFNNPVFRSTVDAVQGG
RDVLRLYGYTEEQPDGLSFPEGQEEPDEHQVATVTLEVLLLRTELSLLLQNTHPRQQALE
QLLE

Sequence of entity 2 (C, D), FASTA

>7UYJ_2 Helicon FP06652 (chains C, D)
DPAIVQCAWAALYCDMQ

Ligands and cofactors

ID	Name	Formula	Copies
WHL	N,N'-(1,4-phenylene)diacetamide	C10 H12 N2 O2	2
NH2	Amino group	H2 N	2

Primary citation

De novo mapping of alpha-helix recognition sites on protein surfaces using unbiased libraries. Li, K., Tokareva, O.S., Thomson, T.M. et al. Proc Natl Acad Sci U S A (2022) 119:e2210435119-e2210435119. DOI 10.1073/pnas.2210435119 · 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
4OYK 2.0 Å, Structure of HOIP PUB domain bound to OTULIN PIM
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

Browse structure collections

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