2EMT: Radixin

Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1. Determined by X-ray diffraction at 2.8 Å resolution. Released 18 Mar 2008.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Mus musculus
Chains: 5
Atoms: 5,565
Mol. weight: 82.63 kDa
Released: 18 Mar 2008

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

Secondary structure: helices and β-sheets

2EMT contains 28 α-helices and 35 β-strands across 5 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: 14 helices, 16 β-strands

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
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
α-helix	242-244	3
β-strand	245-250	6	4
β-strand	254-259	6	4
α-helix	265-266	2
β-strand	267-270	4	4
α-helix	274-293	20
α-helix	297-299	3
α-helix	305-308	4

Chain B: 13 helices, 16 β-strands

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
β-strand	64	1	6
β-strand	70	1	7
β-strand	76-82	7	5
α-helix	89-91	3
α-helix	96-111	16
α-helix	119-134	16
α-helix	155-159	5
α-helix	165-178	14
α-helix	184-195	12
β-strand	203-209	7	8
β-strand	215-221	7	8
β-strand	224-229	6	8
β-strand	238-241	4	8
α-helix	242-244	3
β-strand	245-250	6	8
β-strand	254-259	6	8
β-strand	267-270	4	8
α-helix	274-295	22
α-helix	297-299	3
α-helix	300-303	4
α-helix	305-311	7

Chain C: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	408-411	4	4

Chain D: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	406-407	2
β-strand	408-410	3	8

Chain E: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	406-409	4	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Radixin	A, B	protein	322	Mus musculus	P26043 (AlphaFold model)
P-selectin glycoprotein ligand 1	C, D, E	protein	18		Q62170 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2EMT_1 Radixin (chains A, B)
GSMPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTW
LKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCP
PETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEE
HRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKI
GFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPD
TIEVQQMKAQARVDSSGRIVTD

Sequence of entity 2 (C, D, E), FASTA

>2EMT_2 P-selectin glycoprotein ligand 1 (chains C, D, E)
RLSRKTHMYPVRNYSPTE

Primary citation

Structural basis of PSGL-1 binding to ERM proteins. Takai, Y., Kitano, K., Terawaki, S. et al. Genes Cells (2007) 12:1329-1338. DOI 10.1111/j.1365-2443.2007.01137.x · 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
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…
2YVC 3.2 Å, Crystal structure of the Radixin FERM domain complexed with the NEP cytoplasmic tail

Browse structure collections

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