1SGH: Moesin FERM domain

Moesin FERM domain bound to EBP50 C-terminal peptide. Determined by X-ray diffraction at 3.5 Å resolution. Released 29 Jun 2004.

Method
X-ray diffraction
Resolution
3.5 Å
Organism
Homo sapiens
Chains
2
Atoms
2,482
Mol. weight
39.56 kDa
Released
29 Jun 2004

Explore 1SGH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1SGH contains 8 α-helices and 16 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: 8 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand7-1041
β-strand15-1841
β-strand2512
α-helix26-3611
β-strand45-5061
β-strand5113
β-strand56-5831
β-strand6412
β-strand7013
β-strand76-8271
α-helix89-924
α-helix98-11013
α-helix119-13113
α-helix155-1584
α-helix165-17713
α-helix186-19510
β-strand204-20964
β-strand215-22174
β-strand224-22854
β-strand238-24144
β-strand247-25154
β-strand254-25854
β-strand267-27044
α-helix274-29522

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MoesinAprotein297Homo sapiensP26038 (AlphaFold model)
Ezrin-radixin-moesin binding phosphoprotein 50Bprotein39O14745 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1SGH_1 Moesin (chains A)
MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLK
LNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPE
TAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHR
GMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGF
PWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKP
Sequence of entity 2 (B), FASTA
>1SGH_2 Ezrin-radixin-moesin binding phosphoprotein 50 (chains B)
CLDFNISLAMAKERAHQKRSSKRAPQMDWSKKNELFSNL

Primary citation

The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain. Finnerty, C.M., Chambers, D., Ingraffea, J. et al. J Cell Sci (2004) 117:1547-1552. DOI 10.1242/jcs.01038 · PubMed

Other PDB entries of the same protein (UniProt P26038 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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