1V9D: Core FH2 domain of mouse mDia1

Crystal structure of the core FH2 domain of mouse mDia1. Determined by X-ray diffraction at 2.6 Å resolution. Released 9 Mar 2004.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Mus musculus
Chains: 4
Atoms: 10,079
Mol. weight: 158.4 kDa
Released: 9 Mar 2004

Explore 1V9D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1V9D contains 61 α-helices and 4 β-strands across 4 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: 17 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	837-850	14
α-helix	854-863	10
α-helix	871-880	10
α-helix	884-891	8
α-helix	894-899	6
α-helix	902-911	10
α-helix	916-934	19
α-helix	937-951	15
α-helix	954-958	5
α-helix	987-992	6
β-strand	994	1	1
β-strand	1001	1	1
α-helix	1002-1012	11
α-helix	1020-1023	4
α-helix	1027-1032	6
α-helix	1035-1057	23
α-helix	1059-1062	4
α-helix	1069-1104	36
α-helix	1114-1159	46

Chain B: 17 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	837-848	12
α-helix	854-863	10
α-helix	871-880	10
α-helix	881-883	3
α-helix	884-889	6
α-helix	902-910	9
α-helix	916-952	37
α-helix	954-968	15
α-helix	984-987	4
α-helix	990-992	3
β-strand	994	1	2
β-strand	1001	1	2
α-helix	1002-1013	12
α-helix	1015-1024	10
α-helix	1027-1031	5
α-helix	1035-1057	23
α-helix	1059-1062	4
α-helix	1069-1104	36
α-helix	1114-1146	33

Chain C: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	837-850	14
α-helix	854-862	9
α-helix	871-880	10
α-helix	884-891	8
α-helix	894-896	3
α-helix	902-910	9
α-helix	916-951	36
α-helix	1002-1012	11
α-helix	1027-1032	6
α-helix	1035-1057	23
α-helix	1069-1104	36
α-helix	1114-1146	33

Chain D: 15 helices, 0 β-strands

Element	Residues	Length
α-helix	837-848	12
α-helix	854-863	10
α-helix	871-880	10
α-helix	881-883	3
α-helix	884-891	8
α-helix	902-910	9
α-helix	916-952	37
α-helix	954-962	9
α-helix	990-992	3
α-helix	1002-1013	12
α-helix	1017-1023	7
α-helix	1027-1032	6
α-helix	1035-1057	23
α-helix	1069-1104	36
α-helix	1114-1145	32

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Diaphanous protein homolog 1	A, B, C, D	protein	340	Mus musculus	O08808 (AlphaFold model)

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

>1V9D_1 Diaphanous protein homolog 1 (chains A, B, C, D)
GSKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPE
PEQLKMLSELKEEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQVENIKPEIVSV
TAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLRDTKSADQKMTLL
HFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADVERDVQNFPAAT
DEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHN
FRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQ

Primary citation

The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization. Shimada, A., Nyitrai, M., Vetter, I.R. et al. Mol Cell (2004) 13:511-522. DOI 10.1016/S1097-2765(04)00059-0 · 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
2BNX 2.4 Å, Crystal structure of the dimeric regulatory domain of mouse diaphaneous-related formin…
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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