2YVC: Radixin FERM domain

Crystal structure of the Radixin FERM domain complexed with the NEP cytoplasmic tail. Determined by X-ray diffraction at 3.2 Å resolution. Released 24 Apr 2007.

Method
X-ray diffraction
Resolution
3.2 Å
Organism
Mus musculus
Chains
6
Atoms
7,607
Mol. weight
118.38 kDa
Released
24 Apr 2007

Explore 2YVC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2YVC contains 36 α-helices and 51 β-strands across 6 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: 11 helices, 16 β-strands

ElementResiduesLengthSheet
α-helix41
β-strand5-1061
β-strand17-2041
β-strand2512
α-helix26-3712
α-helix42-443
β-strand45-5061
β-strand5113
β-strand56-5831
α-helix59-602
β-strand6412
β-strand7013
β-strand76-8271
α-helix89-924
α-helix96-11116
α-helix119-13416
α-helix155-1606
α-helix165-17814
α-helix184-19512
β-strand203-20974
β-strand215-22174
β-strand224-22964
β-strand238-24144
β-strand245-25174
β-strand254-25964
β-strand268-27034
α-helix274-29320
Chain B: 13 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix1-44
β-strand5-1065
β-strand15-2065
β-strand2516
α-helix26-3611
β-strand45-5065
β-strand5117
β-strand56-5835
α-helix59-602
β-strand6416
α-helix65-673
β-strand7017
β-strand76-8275
α-helix89-924
α-helix96-11116
α-helix119-13416
α-helix155-1606
α-helix165-17814
α-helix184-19512
β-strand203-21088
β-strand215-22178
β-strand224-22968
β-strand232-241108
α-helix242-2443
β-strand245-25178
β-strand254-25968
α-helix265-2662
β-strand267-27048
α-helix274-29320
Chain C: 11 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand6-1059
β-strand15-1959
β-strand25110
α-helix26-3712
β-strand45-5069
β-strand56-5839
α-helix591
β-strand64110
β-strand75-8289
α-helix89-924
α-helix96-11116
α-helix119-13416
α-helix155-1584
α-helix165-17612
α-helix184-19512
β-strand204111
β-strand207-210411
β-strand215-221711
β-strand224-229611
β-strand232-2411011
α-helix242-2443
β-strand245-251711
β-strand254-259611
α-helix265-2662
β-strand267-270411
α-helix274-29320
Chain D: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand8-1144
Chain E: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand8-1038
Chain F: 1 helix, 2 β-strands
ElementResiduesLengthSheet
β-strand8-10311
α-helix15-173
β-strand18-2035

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RadixinA, B, Cprotein312Mus musculusP26043 (AlphaFold model)
NeprilysinD, E, Fprotein22Q61391 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>2YVC_1 Radixin (chains A, B, C)
GSMPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTW
LKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCP
PETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEE
HRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKI
GFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPD
TIEVQQMKAQAR
Sequence of entity 2 (D, E, F), FASTA
>2YVC_2 Neprilysin (chains D, E, F)
GRSESQMDITDINAPKPKKKQR

Primary citation

Structural basis for type II membrane protein binding by ERM proteins revealed by the radixin-neutral endopeptidase 24.11 (NEP) complex. Terawaki, S., Kitano, K., Hakoshima, T. J Biol Chem (2007) 282:19854-19862. DOI 10.1074/jbc.M609232200 · PubMed

Other PDB entries of the same protein (UniProt P26043 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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