3X23: Radixin complex

Radixin complex. Determined by X-ray diffraction at 2.4 Å resolution. Released 21 Oct 2015.

Method: X-ray diffraction
Resolution: 2.4 Å
Organisms: Mus musculus, Homo sapiens
Chains: 2
Atoms: 2,770
Mol. weight: 39.4 kDa
Released: 21 Oct 2015

Explore 3X23 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3X23 contains 15 α-helices and 17 β-strands across 2 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: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3
β-strand	5-10	6	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
α-helix	71-72	2
β-strand	76-82	7	1
α-helix	89-92	4
α-helix	96-111	16
α-helix	119-134	16
α-helix	155-159	5
α-helix	165-177	13
α-helix	184-195	12
β-strand	204-209	6	4
β-strand	215-220	6	4
β-strand	224-229	6	4
β-strand	238-241	4	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	274-293	20

Chain B: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	569-575	7	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Radixin	A	protein	312	Mus musculus	P26043 (AlphaFold model)
Peptide from Matrix metalloproteinase-14	B	protein	20	Homo sapiens	P50281 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3X23_1 Radixin (chains A)
GSMPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTW
LKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCP
PETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEE
HRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKI
GFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPD
TIEVQQMKAQAR

Sequence of entity 2 (B), FASTA

>3X23_2 Peptide from Matrix metalloproteinase-14 (chains B)
RRHGTPRRLLYCQRSLLDKV

Primary citation

MT1-MMP recognition by ERM proteins and its implication in CD44 shedding. Terawaki, S., Kitano, K., Aoyama, M. et al. Genes Cells (2015) 20:847-859. DOI 10.1111/gtc.12276 · 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…
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
2EMT 2.8 Å, Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule…
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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