4S22: K29 linked di-Ubiquitin

Crystal structure of K29 linked di-Ubiquitin. Determined by X-ray diffraction at 2.3 Å resolution. Released 8 Apr 2015.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Bos taurus
Chains: 4
Atoms: 2,424
Mol. weight: 35.22 kDa
Released: 8 Apr 2015

Explore 4S22 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4S22 contains 17 α-helices and 28 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: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	1
β-strand	12-16	5	1
β-strand	22	1	2
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	1
β-strand	48-49	2	1
α-helix	50-51	2
β-strand	55	1	2
α-helix	57-59	3
β-strand	66-71	6	1

Chain B: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	3
β-strand	12-16	5	3
β-strand	22	1	4
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	3
β-strand	48-49	2	3
α-helix	50-51	2
β-strand	55	1	4
α-helix	57-59	3
β-strand	66-71	6	3
α-helix	72-73	2

Chains C and D: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	5
β-strand	12-16	5	5
β-strand	22	1	6
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	5
β-strand	48-49	2	5
α-helix	50-51	2
β-strand	55	1	6
α-helix	57-59	3
β-strand	66-71	6	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin	A, B, C, D	protein	76	Bos taurus	P63048 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4S22_1 Ubiquitin (chains A, B, C, D)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Primary citation

K29-selective ubiquitin binding domain reveals structural basis of specificity and heterotypic nature of k29 polyubiquitin. Kristariyanto, Y.A., Abdul Rehman, S.A., Campbell, D.G. et al. Mol Cell (2015) 58:83-94. DOI 10.1016/j.molcel.2015.01.041 · PubMed

Other PDB entries of the same protein (UniProt P63048 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4LJO 1.56 Å, Structure of an active ligase (HOIP)/ubiquitin transfer complex
4LJP 2.15 Å, Structure of an active ligase (HOIP-H889A)/ubiquitin transfer complex
2XBB 2.68 Å, Nedd4 HECT:Ub complex
7OBR 2.8 Å, RNC-SRP early complex
7NFX 3.2 Å, Mammalian ribosome nascent chain complex with SRP and SRP receptor in early state A
6ZVK 3.49 Å, The Halastavi arva virus (HalV) intergenic region IRES promotes translation by the…
7A01 3.6 Å, The Halastavi arva virus intergenic region IRES promotes translation by the simplest…

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