1GC6: Radixin ferm domain

Crystal structure of the radixin ferm domain complexed with inositol-(1,4,5)-triphosphate. Determined by X-ray diffraction at 2.9 Å resolution. Released 20 Sept 2000.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
Mus musculus
Chains
1
Atoms
2,506
Mol. weight
35.7 kDa
Ligands
I3P
Released
20 Sept 2000

Explore 1GC6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1GC6 contains 13 α-helices and 17 β-strands across 1 chain. 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: 13 helices, 17 β-strands

ElementResiduesLengthSheet
β-strand5-1171
β-strand14-2071
β-strand2512
α-helix26-3712
α-helix42-443
β-strand45-5061
β-strand5113
β-strand56-5831
α-helix59-602
β-strand6412
α-helix65-673
β-strand7013
β-strand76-8271
α-helix89-924
α-helix96-11116
α-helix119-13315
α-helix155-1584
α-helix165-17713
α-helix184-19512
β-strand204-20964
β-strand215-22174
β-strand224-22854
β-strand238-24144
α-helix242-2443
β-strand245-25065
β-strand255-25955
α-helix265-2662
β-strand267-26935
β-strand27014
α-helix274-29219

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RadixinAprotein297Mus musculusP26043 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1GC6_1 RADIXIN (chains A)
MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLK
LNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPE
TAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHR
GMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGF
PWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKP

Ligands and cofactors

IDNameFormulaCopies
I3PD-myo-inositol-1,4,5-triphosphateC6 H15 O15 P31

Primary citation

Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. Hamada, K., Shimizu, T., Matsui, T. et al. EMBO J (2000) 19:4449-4462. DOI 10.1093/emboj/19.17.4449 · 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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