2D11: Radixin FERM domain

Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide. Determined by X-ray diffraction at 2.81 Å resolution. Released 18 Jul 2006.

Method: X-ray diffraction
Resolution: 2.81 Å
Organism: Mus musculus
Chains: 8
Atoms: 10,601
Mol. weight: 161.77 kDa
Released: 18 Jul 2006

Explore 2D11 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2D11 contains 58 α-helices and 63 β-strands across 8 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
α-helix	4	1
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
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	155-159	5
α-helix	165-178	14
α-helix	184-195	12
β-strand	204-209	6	4
β-strand	215-221	7	4
β-strand	224-229	6	4
β-strand	232-241	10	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: 11 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
α-helix	65-67	3
β-strand	70	1	7
β-strand	76-82	7	5
α-helix	89-92	4
α-helix	96-111	16
α-helix	119-134	16
α-helix	155-158	4
α-helix	165-178	14
α-helix	184-195	12
β-strand	204-209	6	8
β-strand	215-220	6	8
β-strand	224-229	6	8
β-strand	232-241	10	8
α-helix	242-244	3
β-strand	245-251	7	8
β-strand	254-259	6	8
β-strand	267-270	4	8
α-helix	274-293	20

Chain C: 13 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	4	1
β-strand	5-10	6	9
β-strand	15-20	6	9
β-strand	25	1	10
α-helix	26-37	12
β-strand	45-50	6	9
β-strand	56-58	3	9
α-helix	59-60	2
β-strand	64	1	10
α-helix	66-68	3
β-strand	76-82	7	9
α-helix	89-92	4
α-helix	96-111	16
α-helix	119-134	16
α-helix	155-158	4
α-helix	165-177	13
α-helix	184-195	12
β-strand	204-209	6	11
β-strand	215-220	6	11
β-strand	224-229	6	11
β-strand	232	1	11
β-strand	238-241	4	11
α-helix	242-244	3
β-strand	245-250	6	11
β-strand	254-259	6	11
α-helix	265-266	2
β-strand	267-270	4	11
α-helix	274-295	22

Chain D: 13 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	12
β-strand	14-20	7	12
β-strand	25	1	13
α-helix	26-37	12
α-helix	42-44	3
β-strand	45-50	6	12
β-strand	51	1	14
β-strand	56-58	3	12
α-helix	59-60	2
β-strand	64	1	13
α-helix	65-67	3
β-strand	70	1	14
β-strand	76-82	7	12
α-helix	89-92	4
α-helix	96-111	16
α-helix	119-134	16
α-helix	155-160	6
α-helix	165-177	13
α-helix	184-196	13
β-strand	204-209	6	15
β-strand	215-221	7	15
β-strand	224-229	6	15
β-strand	236-241	6	15
α-helix	242-244	3
β-strand	245-251	7	15
β-strand	254-259	6	15
α-helix	265-266	2
β-strand	267-270	4	15
α-helix	274-293	20

Chains E, G and H: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	322-324	3
α-helix	327-336	10

Chain F: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	327-336	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Radixin	A, B, C, D	protein	312	Mus musculus	P26043 (AlphaFold model)
Na(+)/H(+) exchange regulatory cofactor NHE-RF2	E, F, G, H	protein	28		Q15599 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>2D11_1 Radixin (chains A, B, C, D)
GSMPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTW
LKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCP
PETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEE
HRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKI
GFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPD
TIEVQQMKAQAR

Sequence of entity 2 (E, F, G, H), FASTA

>2D11_2 Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (chains E, F, G, H)
KEKARAMRVNKRAPQMDWNRKREIFSNF

Primary citation

Structural basis for NHERF recognition by ERM proteins. Terawaki, S., Maesaki, R., Hakoshima, T. Structure (2006) 14:777-789. DOI 10.1016/j.str.2006.01.015 · 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
2EMT 2.8 Å, Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule…
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

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