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
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4 | 1 | |
| β-strand | 5-10 | 6 | 1 |
| β-strand | 17-20 | 4 | 1 |
| β-strand | 25 | 1 | 2 |
| α-helix | 26-37 | 12 | |
| α-helix | 42-44 | 3 | |
| β-strand | 45-50 | 6 | 1 |
| β-strand | 51 | 1 | 3 |
| β-strand | 56-58 | 3 | 1 |
| α-helix | 59-60 | 2 | |
| β-strand | 64 | 1 | 2 |
| β-strand | 70 | 1 | 3 |
| β-strand | 76-82 | 7 | 1 |
| α-helix | 89-92 | 4 | |
| α-helix | 96-111 | 16 | |
| α-helix | 119-134 | 16 | |
| α-helix | 155-160 | 6 | |
| α-helix | 165-178 | 14 | |
| α-helix | 184-195 | 12 | |
| β-strand | 203-209 | 7 | 4 |
| β-strand | 215-221 | 7 | 4 |
| β-strand | 224-229 | 6 | 4 |
| β-strand | 238-241 | 4 | 4 |
| β-strand | 245-251 | 7 | 4 |
| β-strand | 254-259 | 6 | 4 |
| β-strand | 268-270 | 3 | 4 |
| α-helix | 274-293 | 20 | |
Chain B: 13 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-4 | 4 | |
| β-strand | 5-10 | 6 | 5 |
| β-strand | 15-20 | 6 | 5 |
| β-strand | 25 | 1 | 6 |
| α-helix | 26-36 | 11 | |
| β-strand | 45-50 | 6 | 5 |
| β-strand | 51 | 1 | 7 |
| β-strand | 56-58 | 3 | 5 |
| α-helix | 59-60 | 2 | |
| β-strand | 64 | 1 | 6 |
| α-helix | 65-67 | 3 | |
| β-strand | 70 | 1 | 7 |
| β-strand | 76-82 | 7 | 5 |
| α-helix | 89-92 | 4 | |
| α-helix | 96-111 | 16 | |
| α-helix | 119-134 | 16 | |
| α-helix | 155-160 | 6 | |
| α-helix | 165-178 | 14 | |
| α-helix | 184-195 | 12 | |
| β-strand | 203-210 | 8 | 8 |
| β-strand | 215-221 | 7 | 8 |
| β-strand | 224-229 | 6 | 8 |
| β-strand | 232-241 | 10 | 8 |
| α-helix | 242-244 | 3 | |
| β-strand | 245-251 | 7 | 8 |
| β-strand | 254-259 | 6 | 8 |
| α-helix | 265-266 | 2 | |
| β-strand | 267-270 | 4 | 8 |
| α-helix | 274-293 | 20 | |
Chain C: 11 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-10 | 5 | 9 |
| β-strand | 15-19 | 5 | 9 |
| β-strand | 25 | 1 | 10 |
| α-helix | 26-37 | 12 | |
| β-strand | 45-50 | 6 | 9 |
| β-strand | 56-58 | 3 | 9 |
| α-helix | 59 | 1 | |
| β-strand | 64 | 1 | 10 |
| β-strand | 75-82 | 8 | 9 |
| α-helix | 89-92 | 4 | |
| α-helix | 96-111 | 16 | |
| α-helix | 119-134 | 16 | |
| α-helix | 155-158 | 4 | |
| α-helix | 165-176 | 12 | |
| α-helix | 184-195 | 12 | |
| β-strand | 204 | 1 | 11 |
| β-strand | 207-210 | 4 | 11 |
| β-strand | 215-221 | 7 | 11 |
| β-strand | 224-229 | 6 | 11 |
| β-strand | 232-241 | 10 | 11 |
| α-helix | 242-244 | 3 | |
| β-strand | 245-251 | 7 | 11 |
| β-strand | 254-259 | 6 | 11 |
| α-helix | 265-266 | 2 | |
| β-strand | 267-270 | 4 | 11 |
| α-helix | 274-293 | 20 | |
Chain D: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-11 | 4 | 4 |
Chain E: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-10 | 3 | 8 |
Chain F: 1 helix, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-10 | 3 | 11 |
| α-helix | 15-17 | 3 | |
| β-strand | 18-20 | 3 | 5 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Radixin | A, B, C | protein | 312 | Mus musculus | P26043 (AlphaFold model) |
| Neprilysin | D, E, F | protein | 22 | | Q61391 (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:
- 2ZPY 2.1 Å, Crystal structure of the mouse radxin FERM domain complexed with the mouse CD44…
- 3X23 2.4 Å, Radixin complex
- 1J19 2.4 Å, Crystal structure of the radxin FERM domain complexed with the ICAM-2 cytoplasmic peptide
- 2D10 2.5 Å, Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail…
- 1GC7 2.8 Å, Crystal structure of the radixin ferm domain
- 2D2Q 2.8 Å, Crystal structure of the dimerized radixin FERM domain
- 2EMT 2.8 Å, Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule…
- 2D11 2.81 Å, Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail…
- 1GC6 2.9 Å, Crystal structure of the radixin ferm domain complexed with inositol-(1,4,5)-triphosphate
- 2EMS 2.9 Å, Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule…
Browse structure collections
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