2F31: Diaphanous protein homolog 1

Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex. Determined by X-ray diffraction at 2.1 Å resolution. Released 30 May 2006.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Mus musculus
Chains: 2
Atoms: 2,087
Mol. weight: 28.7 kDa
Released: 30 May 2006

Explore 2F31 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2F31 contains 14 α-helices and 0 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: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	136-143	8
α-helix	149-165	17
α-helix	168-190	23
α-helix	201-215	15
α-helix	219-226	8
α-helix	231-236	6
α-helix	244-258	15
α-helix	266-281	16
α-helix	287-291	5
α-helix	299-313	15
α-helix	319-331	13
α-helix	334-343	10
α-helix	347-366	20

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Diaphanous protein homolog 1	A	protein	233	Mus musculus	Q3US76 (AlphaFold model)
Diaphanous protein homolog 1	B	protein	20	Mus musculus	O08808 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2F31_1 Diaphanous protein homolog 1 (chains A)
SAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKE
ETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLL
SALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLINALIT
PAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDL

Sequence of entity 2 (B), FASTA

>2F31_2 Diaphanous protein homolog 1 (chains B)
DETGVMDSLLEALQSGAAFR

Primary citation

Structure of the Autoinhibitory Switch in Formin mDia1. Nezami, A.G., Poy, F., Eck, M.J. Structure (2006) 14:257-263. DOI 10.1016/j.str.2005.12.003 · PubMed

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