1EF1: Moesin ferm domain/tail domain complex

Crystal structure of the moesin ferm domain/tail domain complex. Determined by X-ray diffraction at 1.9 Å resolution. Released 10 May 2000.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,688
Mol. weight: 91.02 kDa
Released: 10 May 2000

Explore 1EF1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1EF1 contains 36 α-helices and 37 β-strands across 4 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: 12 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	1
β-strand	14-20	7	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
β-strand	161	1	4
α-helix	165-178	14
α-helix	184-195	12
β-strand	204-209	6	5
β-strand	215-221	7	5
β-strand	224-229	6	5
β-strand	238-241	4	5
α-helix	242-244	3
β-strand	245-251	7	5
β-strand	254-259	6	5
β-strand	267-270	4	5
α-helix	274-295	22

Chain B: 12 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	6
β-strand	15-20	6	6
β-strand	25	1	7
α-helix	26-37	12
α-helix	42-44	3
β-strand	45-50	6	6
β-strand	51	1	8
β-strand	56-58	3	6
α-helix	59-60	2
β-strand	64	1	7
β-strand	70	1	8
β-strand	76-82	7	6
α-helix	89-92	4
α-helix	96-111	16
α-helix	119-134	16
α-helix	155-160	6
β-strand	161	1	9
α-helix	165-178	14
α-helix	184-195	12
β-strand	204-209	6	10
β-strand	215-221	7	10
β-strand	224-229	6	10
β-strand	232	1	10
β-strand	238-241	4	10
α-helix	242-244	3
β-strand	245-251	7	10
β-strand	254-259	6	10
α-helix	265-266	2
β-strand	267-270	4	10
α-helix	274-295	22

Chain C: 6 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	504-507	4
α-helix	511-514	4
α-helix	516-530	15
β-strand	533	1	4
α-helix	540-550	11
α-helix	555-562	8
α-helix	567-575	9

Chain D: 6 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	504-507	4
α-helix	511-514	4
α-helix	516-530	15
β-strand	533	1	9
α-helix	540-550	11
α-helix	555-562	8
α-helix	567-576	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Moesin	A, B	protein	294	Homo sapiens	P26038 (AlphaFold model)
Moesin	C, D	protein	90	Homo sapiens	P26038 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1EF1_1 MOESIN (chains A, B)
TISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNK
KVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAV
LLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGML
REDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWS
EIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKP

Sequence of entity 2 (C, D), FASTA

>1EF1_2 MOESIN (chains C, D)
AEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAE
NMRLGRDKYKTLRQIRQGNTKQRIDEFESM

Primary citation

Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Pearson, M.A., Reczek, D., Bretscher, A. et al. Cell (2000) 101:259-270. DOI 10.1016/S0092-8674(00)80836-3 · PubMed

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

8CIS 1.52 Å, The FERM domain of human moesin with two bound peptides identified by phage display
6TXQ 1.73 Å, The high resolution structure of the FERM domain and helical linker of human moesin
8XZ5 1.8 Å, SARS-CoV-2 S and moesin complex structure
8CIR 1.85 Å, The FERM domain of human moesin with a bound peptide identified by phage display
6TXS 2.2 Å, The structure of the FERM domain and helical linker of human moesin bound to a CD44…
8CIU 2.39 Å, The FERM domain of human moesin mutant H288A
8CIT 2.54 Å, The FERM domain of human moesin mutant L281R
1E5W 2.7 Å, Structure of isolated FERM domain and first long helix of moesin
1SGH 3.5 Å, Moesin FERM domain bound to EBP50 C-terminal peptide

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