5Y4D: AnkB Ankyrin Repeats

Crystal Structure of AnkB Ankyrin Repeats in Complex with AnkR/AnkB Chimeric Autoinhibition Segment. Determined by X-ray diffraction at 3.3 Å resolution. Released 13 Sept 2017.

Method
X-ray diffraction
Resolution
3.3 Å
Organisms
Mus musculus, Homo sapiens
Chains
1
Atoms
5,069
Mol. weight
78.99 kDa
Released
13 Sept 2017

Explore 5Y4D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5Y4D contains 45 α-helices and 2 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 A: 45 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix1602-161312
α-helix1623-16253
α-helix1629-16313
α-helix2029-204113
α-helix2044-20529
α-helix2067-20748
α-helix2077-208610
α-helix2100-21078
α-helix2110-21189
α-helix2133-21397
α-helix2143-21519
α-helix2166-21738
α-helix2176-21849
α-helix2192-220211
α-helix2205-22117
α-helix2225-22273
α-helix2236-22438
α-helix2246-22549
β-strand226311
β-strand226711
α-helix2269-22768
α-helix2279-22879
α-helix2302-23087
α-helix2312-23209
α-helix2335-23417
α-helix2345-23539
α-helix2368-23747
α-helix2378-23869
α-helix2401-24077
α-helix2411-24199
α-helix2434-24407
α-helix2444-24529
α-helix2467-24748
α-helix2477-24859
α-helix2495-24973
α-helix2500-25067
α-helix2510-25189
α-helix2533-25408
α-helix2543-25519
α-helix2566-25738
α-helix2576-25849
α-helix2599-26057
α-helix2609-261810
α-helix2632-26387
α-helix2642-26509
α-helix2665-26728
α-helix2675-26817

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ankyrin-1,Ankyrin-2,Ankyrin-2Aprotein731Mus musculus, Homo sapiensQ01484 (AlphaFold model), Q02357 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5Y4D_1 Ankyrin-1,Ankyrin-2,Ankyrin-2 (chains A)
GPGSEFCADQYWNEVAVIDAIPLAATEHDTMLEMSDMQVWSAGDHPPIVSEEDISGSLVP
RGSGSKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQE
LLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENH
IDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARK
DDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFT
ARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERG
APLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTK
LLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMG
HLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLH
IASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKK
GFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASP
HATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLL
DKGANIHMSTK

Primary citation

Autoinhibition of ankyrin-B/G membrane target bindings by intrinsically disordered segments from the tail regions. Chen, K., Li, J., Wang, C. et al. Elife (2017) 6. DOI 10.7554/eLife.29150 · PubMed

Other PDB entries of the same protein (UniProt Q01484 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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