3OBV: Autoinhibited Formin mDia1 Structure

Autoinhibited Formin mDia1 Structure. Determined by X-ray diffraction at 2.75 Å resolution. Released 24 Nov 2010.

Method: X-ray diffraction
Resolution: 2.75 Å
Organism: Mus musculus
Chains: 8
Atoms: 24,224
Mol. weight: 365.9 kDa
Released: 24 Nov 2010

Explore 3OBV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3OBV contains 168 α-helices and 28 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: 17 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	135-143	9
α-helix	149-165	17
α-helix	168-194	27
α-helix	202-215	14
α-helix	219-226	8
α-helix	231-237	7
α-helix	244-259	16
α-helix	266-281	16
α-helix	287-291	5
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	397-409	13
α-helix	417-433	17
α-helix	436-438	3
β-strand	447-451	5	1

Chain B: 17 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	134-143	10
α-helix	149-165	17
α-helix	168-191	24
α-helix	202-215	14
α-helix	219-227	9
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	347-377	31
α-helix	381-392	12
α-helix	398-408	11
α-helix	417-433	17
α-helix	436-438	3
β-strand	447-451	5	1

Chain C: 17 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	133-143	11
α-helix	149-165	17
α-helix	168-193	26
α-helix	202-215	14
α-helix	219-226	8
α-helix	231-237	7
α-helix	244-259	16
α-helix	266-281	16
α-helix	287-291	5
α-helix	299-313	15
α-helix	319-332	14
α-helix	334-341	8
α-helix	347-377	31
α-helix	381-392	12
α-helix	397-409	13
α-helix	417-433	17
α-helix	436-438	3
β-strand	447-451	5	8

Chain D: 17 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	135-143	9
α-helix	149-165	17
α-helix	168-194	27
α-helix	201-215	15
α-helix	219-227	9
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	319-332	14
α-helix	334-341	8
α-helix	347-377	31
α-helix	381-392	12
α-helix	398-408	11
α-helix	417-433	17
α-helix	436-438	3
β-strand	447-451	5	8

Chain E: 28 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	761	1
β-strand	762	1	2
α-helix	763	1
α-helix	767-768	2
β-strand	769-770	2	3
α-helix	781-783	3
α-helix	786-789	4
α-helix	794-801	8
β-strand	803	1	2
α-helix	830-832	3
α-helix	837-850	14
α-helix	854-863	10
α-helix	871-880	10
α-helix	881-883	3
α-helix	884-891	8
α-helix	897-899	3
α-helix	902-910	9
α-helix	916-933	18
α-helix	937-951	15
α-helix	954-970	17
β-strand	982	1	4
α-helix	984-986	3
α-helix	987-990	4
β-strand	994	1	5
β-strand	1001	1	5
α-helix	1002-1013	12
α-helix	1015-1019	5
α-helix	1020-1023	4
α-helix	1027-1030	4
α-helix	1035-1057	23
α-helix	1059-1062	4
α-helix	1069-1104	36
α-helix	1114-1166	53
α-helix	1181-1191	11

Chain F: 22 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	762	1	6
β-strand	769	1	4
α-helix	772-775	4
α-helix	786-789	4
α-helix	792-801	10
β-strand	803	1	6
α-helix	837-850	14
α-helix	854-863	10
α-helix	871-880	10
α-helix	881-883	3
α-helix	884-888	5
α-helix	902-912	11
α-helix	916-933	18
α-helix	937-952	16
α-helix	954-970	17
β-strand	981-982	2	3
α-helix	984-992	9
β-strand	994	1	7
β-strand	1001	1	7
α-helix	1002-1013	12
α-helix	1015-1022	8
α-helix	1027-1032	6
α-helix	1035-1056	22
α-helix	1059-1062	4
α-helix	1069-1104	36
α-helix	1109-1111	3
α-helix	1114-1166	53
α-helix	1181-1191	11

Chain G: 26 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	761	1
β-strand	762	1	9
α-helix	763	1
α-helix	767-768	2
β-strand	769-770	2	10
α-helix	781-783	3
α-helix	786-789	4
α-helix	794-801	8
β-strand	803	1	9
α-helix	830-832	3
α-helix	837-850	14
α-helix	854-863	10
α-helix	871-880	10
α-helix	884-891	8
α-helix	897-899	3
α-helix	902-910	9
α-helix	916-933	18
α-helix	937-951	15
α-helix	954-970	17
β-strand	981-982	2	11
α-helix	984-992	9
β-strand	994	1	12
β-strand	1001	1	12
α-helix	1002-1013	12
α-helix	1015-1019	5
α-helix	1020-1023	4
α-helix	1027-1030	4
α-helix	1035-1057	23
α-helix	1059-1062	4
α-helix	1069-1104	36
α-helix	1114-1166	53
α-helix	1181-1191	11

Chain H: 24 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	761	1
β-strand	762	1	13
α-helix	763	1
β-strand	769-770	2	11
α-helix	772-775	4
α-helix	786-789	4
α-helix	792-801	10
β-strand	803	1	13
α-helix	837-850	14
α-helix	854-863	10
α-helix	871-880	10
α-helix	881-883	3
α-helix	884-888	5
α-helix	902-912	11
α-helix	916-933	18
α-helix	937-952	16
α-helix	954-970	17
β-strand	981-982	2	10
α-helix	984-992	9
β-strand	994	1	14
β-strand	1001	1	14
α-helix	1002-1013	12
α-helix	1015-1022	8
α-helix	1027-1030	4
α-helix	1035-1056	22
α-helix	1059-1062	4
α-helix	1069-1104	36
α-helix	1109-1111	3
α-helix	1114-1166	53
α-helix	1181-1191	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein diaphanous homolog 1	A, B, C, D	protein	327	Mus musculus	O08808 (AlphaFold model)
Protein diaphanous homolog 1	E, F, G, H	protein	457	Mus musculus	O08808 (AlphaFold model)

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

>3OBV_1 Protein diaphanous homolog 1 (chains A, B, C, D)
ESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLH
DEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDA
AKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLIN
ALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLKGR
LDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECVS
QIVLHKNGTDPDFKCRHLQIDIERLVD

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

>3OBV_2 Protein diaphanous homolog 1 (chains E, F, G, H)
KKVYKPEVQLRRPNWSKFVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSKAK
KDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTES
MIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQ
VENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLRD
TKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADV
ERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKL
SVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQQKREQLIDM
NAEGDETGVMDSLLEALQSGAAFRRKRGPRQVNRKAG

Primary citation

Crystal structure of the Formin mDia1 in autoinhibited conformation. Otomo, T., Tomchick, D.R., Otomo, C. et al. PLoS One (2010) 5:e12896-e12896. DOI 10.1371/journal.pone.0012896 · 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…
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
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

Browse structure collections

About this viewer

MolViewer shows 3OBV directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.