2BNX: Diaphanous protein homolog 1

Crystal structure of the dimeric regulatory domain of mouse diaphaneous-related formin (DRF), mDia1. Determined by X-ray diffraction at 2.4 Å resolution. Released 13 Jun 2005.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: MUS MUSCULUS
Chains: 2
Atoms: 5,687
Mol. weight: 89.23 kDa
Released: 13 Jun 2005

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

Secondary structure: helices and β-sheets

2BNX contains 36 α-helices and 2 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: 18 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	219-227	9
α-helix	231-237	7
α-helix	244-258	15
α-helix	266-281	16
α-helix	287-292	6
α-helix	299-313	15
α-helix	319-331	13
α-helix	334-341	8
α-helix	347-377	31
α-helix	381-392	12
α-helix	397-408	12
α-helix	418-433	16
α-helix	436-438	3
α-helix	464-469	6

Chain B: 18 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	136-143	8
α-helix	149-165	17
α-helix	168-191	24
α-helix	194-196	3
α-helix	201-215	15
α-helix	219-226	8
α-helix	231-237	7
α-helix	244-259	16
α-helix	266-281	16
α-helix	287-293	7
α-helix	299-313	15
α-helix	319-331	13
α-helix	334-341	8
α-helix	347-371	25
α-helix	381-392	12
α-helix	397-408	12
α-helix	417-434	18
β-strand	436	1	1
β-strand	439	1	1
α-helix	452-473	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Diaphanous protein homolog 1	A, B	protein	386	MUS MUSCULUS	O08808 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2BNX_1 DIAPHANOUS PROTEIN HOMOLOG 1 (chains A, B)
ESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLH
DEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDA
AKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLIN
ALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLKGR
LDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECVS
QIVLHKNGTDPDFKCRHLQIDIERLVDQMIDKTKVEKSEAKATELEKKLDSELTARHELQ
VEMKKMENDFEQKLQDLQGEKDALDS

Primary citation

Structural Basis of Rho Gtpase-Mediated Activation of the Formin Mdia1. Otomo, T., Otomo, C., Tomchick, D.R. et al. Mol Cell (2005) 18:273. DOI 10.1016/J.MOLCEL.2005.04.002 · PubMed

Other PDB entries of the same protein (UniProt O08808 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2V8F 1.1 Å, Mouse Profilin IIa in complex with a double repeat from the FH1 domain of mDia1
4UWX 1.65 Å, Structure of liprin-alpha3 in complex with mDia1 Diaphanous- inhibitory domain
2F31 2.1 Å, Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex
1V9D 2.6 Å, Crystal structure of the core FH2 domain of mouse mDia1
3EG5 2.7 Å, Crystal structure of MDIA1-TSH GBD-FH3 in complex with CDC42-GMPPNP
3OBV 2.75 Å, Autoinhibited Formin mDia1 Structure
1Z2C 3.0 Å, Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP
3O4X 3.2 Å, Crystal structure of complex between amino and carboxy terminal fragments of mDia1
2BAP 3.3 Å, Crystal structure of the N-terminal mDia1 Armadillo Repeat Region and Dimerisation…
9B3D 3.41 Å, mDia1 in the middle of F-actin
8RU2 3.49 Å, Structure of the F-actin barbed end bound by formin mDia1
9B27 3.51 Å, Dia1 at the Barbed End of F-Actin

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