5B4N: F-box only protein 2

Name: PDB 5B4N: Structure analysis of function associated loop mutant of substrate recognition domain of Fbs1 ubiquitin ligase
Published: 2016-09-14
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

Structure analysis of function associated loop mutant of substrate recognition domain of Fbs1 ubiquitin ligase. Determined by X-ray diffraction at 2.3 Å resolution. Released 14 Sept 2016.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Mus musculus
Chains: 2
Atoms: 2,955
Mol. weight: 47.25 kDa
Released: 14 Sept 2016

Explore 5B4N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5B4N contains 14 α-helices and 28 β-strands across 2 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: 7 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	140	1
β-strand	141-142	2	1
α-helix	146-149	4
β-strand	150-154	5	2
α-helix	155-156	2
α-helix	157-160	4
β-strand	170-174	5	2
β-strand	180-186	7	1
α-helix	194-195	2
α-helix	196-200	5
β-strand	204-211	8	2
β-strand	213	1	3
β-strand	216	1	3
β-strand	218-220	3	4
β-strand	221-227	7	1
β-strand	233-237	5	1
α-helix	239-241	3
β-strand	242-244	3	4
β-strand	253-259	7	2
β-strand	268-274	7	1
β-strand	285	1	4
β-strand	288-296	9	2

Chain B: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	140	1
β-strand	141-142	2	5
α-helix	146-149	4
β-strand	150-154	5	6
α-helix	155-156	2
α-helix	159-162	4
β-strand	170-174	5	6
β-strand	180-186	7	5
α-helix	194-195	2
α-helix	196-200	5
β-strand	204-211	8	6
β-strand	218-220	3	7
β-strand	221-227	7	5
β-strand	233-237	5	5
α-helix	239-241	3
β-strand	242-244	3	7
β-strand	253-259	7	6
β-strand	268-274	7	5
β-strand	285	1	7
β-strand	288-296	9	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
F-box only protein 2	A, B	protein	203	Mus musculus	Q80UW2 (AlphaFold model), Q9H4M3 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5B4N_1 F-box only protein 2 (chains A, B)
MGSSHHHHHHSSGLVPRGSHMFYFLSKRRRNLLRNPCGEEDLEGWSLDVNGGDGWKVEEL
SRDQRKEFPNDQVKKYFVTSYYTCRKAQVIDLQAEGYWEELLDTTQPAIVVKDWYSGRPD
CGSKYQLTVRLLSENEDVLAEFQPDPATIQQKSDAKWREISHTFIDYGPGVRFVRFEHGG
VDTHYWAGWYGPRVTNSSVWVEP

Primary citation

Structural analysis of a function-associated loop mutant of the substrate-recognition domain of Fbs1 ubiquitin ligase. Nishio, K., Yoshida, Y., Tanaka, K. et al. Acta Crystallogr F Struct Biol Commun (2016) 72:619-626. DOI 10.1107/S2053230X16011018 · PubMed

Other PDB entries of the same protein (UniProt Q80UW2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2RJ2 1.7 Å, Crystal Structure of the Sugar Recognizing SCF Ubiquitin Ligase at 1.7 Resolution
1UMH 2.0 Å, Structural basis of sugar-recognizing ubiquitin ligase
1UMI 2.4 Å, Structural basis of sugar-recognizing ubiquitin ligase
2E31 2.4 Å, Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase
2E33 2.7 Å, Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase
2E32 3.52 Å, Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase

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