The FERM domain of human moesin mutant L281R. Determined by X-ray diffraction at 2.54 Å resolution. Released 1 Mar 2023.
Explore 8CIT in 3D Show helices and sheets RCSB PDB PDBe
8CIT contains 44 α-helices and 48 β-strands across 3 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-10 | 6 | 1 |
| β-strand | 15-20 | 6 | 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 |
| α-helix | 65-67 | 3 | |
| 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 | 204-209 | 6 | 4 |
| β-strand | 215-221 | 7 | 4 |
| β-strand | 224-229 | 6 | 4 |
| β-strand | 236-241 | 6 | 4 |
| α-helix | 242-244 | 3 | |
| β-strand | 245-251 | 7 | 4 |
| β-strand | 254-259 | 6 | 4 |
| α-helix | 265-266 | 2 | |
| β-strand | 267-270 | 4 | 4 |
| α-helix | 274-295 | 22 | |
| α-helix | 297-299 | 3 | |
| α-helix | 300-339 | 40 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-10 | 6 | 5 |
| β-strand | 15-20 | 6 | 5 |
| β-strand | 25 | 1 | 6 |
| α-helix | 26-37 | 12 | |
| α-helix | 42-44 | 3 | |
| 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 | 204-209 | 6 | 8 |
| β-strand | 215-221 | 7 | 8 |
| β-strand | 224-229 | 6 | 8 |
| β-strand | 236-241 | 6 | 8 |
| β-strand | 245-250 | 6 | 8 |
| β-strand | 254-259 | 6 | 8 |
| α-helix | 265-266 | 2 | |
| β-strand | 267-270 | 4 | 8 |
| α-helix | 274-295 | 22 | |
| α-helix | 297-299 | 3 | |
| α-helix | 300-342 | 43 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-10 | 6 | 9 |
| β-strand | 15-20 | 6 | 9 |
| β-strand | 25 | 1 | 10 |
| α-helix | 26-37 | 12 | |
| α-helix | 42-44 | 3 | |
| β-strand | 45-50 | 6 | 9 |
| β-strand | 51 | 1 | 11 |
| β-strand | 56-58 | 3 | 9 |
| α-helix | 59-60 | 2 | |
| β-strand | 64 | 1 | 10 |
| α-helix | 65-67 | 3 | |
| β-strand | 70 | 1 | 11 |
| β-strand | 76-82 | 7 | 9 |
| 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 | 204-209 | 6 | 12 |
| β-strand | 215-221 | 7 | 12 |
| β-strand | 224-229 | 6 | 12 |
| β-strand | 236-241 | 6 | 12 |
| α-helix | 242-244 | 3 | |
| β-strand | 245-250 | 6 | 12 |
| β-strand | 254-259 | 6 | 12 |
| α-helix | 265-266 | 2 | |
| β-strand | 267-270 | 4 | 12 |
| α-helix | 274-294 | 21 | |
| α-helix | 297-299 | 3 | |
| α-helix | 300-326 | 27 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Moesin | A, B, C | protein | 347 | Homo sapiens | P26038 (AlphaFold model) |
>8CIT_1 Moesin (chains A, B, C) SMPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWL KLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPP ETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEH RGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIG FPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRIRALCMGNHELYMRRRKPDT IEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEE
Discovery of FERM domain protein-protein interaction inhibitors for MSN and CD44 as a potential therapeutic approach for Alzheimer's disease. Du, Y., Bradshaw, W.J., Leisner, T.M. et al. J Biol Chem (2023) 299:105382-105382. DOI 10.1016/j.jbc.2023.105382 · PubMed
Other PDB entries of the same protein (UniProt P26038 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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