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

ElementResiduesLengthSheet
β-strand5-1061
β-strand15-2061
β-strand2512
α-helix26-3712
α-helix42-443
β-strand45-5061
β-strand5113
β-strand56-5831
α-helix59-602
β-strand6412
β-strand7013
β-strand76-8271
α-helix89-924
α-helix96-11116
α-helix119-13416
α-helix155-1606
α-helix165-17814
α-helix184-19512
β-strand203-20974
β-strand215-22174
β-strand224-22964
β-strand238-24144
α-helix242-2443
β-strand245-25064
β-strand254-25964
α-helix265-2662
β-strand267-27044
α-helix274-29320
α-helix297-2993
α-helix305-3084
Chain B: 13 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand5-1065
β-strand15-2065
β-strand2516
α-helix26-3712
α-helix42-443
β-strand45-5065
β-strand5117
β-strand56-5835
β-strand6416
β-strand7017
β-strand76-8275
α-helix89-913
α-helix96-11116
α-helix119-13416
α-helix155-1595
α-helix165-17814
α-helix184-19512
β-strand203-20978
β-strand215-22178
β-strand224-22968
β-strand238-24148
α-helix242-2443
β-strand245-25068
β-strand254-25968
β-strand267-27048
α-helix274-29522
α-helix297-2993
α-helix300-3034
α-helix305-3117
Chain C: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand408-41144
Chain D: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix406-4072
β-strand408-41038
Chain E: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand406-40941

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RadixinA, Bprotein322Mus musculusP26043 (AlphaFold model)
P-selectin glycoprotein ligand 1C, D, Eprotein18Q62170 (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:

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