3O4X: Protein diaphanous homolog 1
Crystal structure of complex between amino and carboxy terminal fragments of mDia1. Determined by X-ray diffraction at 3.2 Å resolution. Released 13 Oct 2010.
- Method
- X-ray diffraction
- Resolution
- 3.2 Å
- Organism
- Mus musculus
- Chains
- 8
- Atoms
- 24,335
- Mol. weight
- 367.47 kDa
- Released
- 13 Oct 2010
Explore 3O4X in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3O4X contains 161 α-helices and 30 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: 16 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 136-143 | 8 | |
| α-helix | 149-165 | 17 | |
| α-helix | 168-190 | 23 | |
| α-helix | 202-215 | 14 | |
| α-helix | 219-225 | 7 | |
| α-helix | 231-237 | 7 | |
| α-helix | 244-258 | 15 | |
| α-helix | 266-281 | 16 | |
| α-helix | 287-291 | 5 | |
| α-helix | 299-313 | 15 | |
| α-helix | 319-332 | 14 | |
| α-helix | 334-342 | 9 | |
| α-helix | 347-377 | 31 | |
| α-helix | 381-392 | 12 | |
| α-helix | 397-410 | 14 | |
| α-helix | 418-433 | 16 | |
| β-strand | 447-448 | 2 | 1 |
Chain B: 16 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 136-143 | 8 | |
| α-helix | 149-165 | 17 | |
| α-helix | 168-189 | 22 | |
| α-helix | 202-215 | 14 | |
| α-helix | 219-227 | 9 | |
| α-helix | 231-236 | 6 | |
| α-helix | 244-258 | 15 | |
| 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 | 397-408 | 12 | |
| α-helix | 418-433 | 16 | |
| β-strand | 447-448 | 2 | 2 |
Chain C: 16 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| 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 | 266-280 | 15 | |
| 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 | 397-408 | 12 | |
| α-helix | 418-433 | 16 | |
| β-strand | 448-449 | 2 | 2 |
Chain D: 18 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 136-144 | 9 | |
| α-helix | 149-165 | 17 | |
| α-helix | 168-190 | 23 | |
| α-helix | 203-215 | 13 | |
| α-helix | 219-227 | 9 | |
| α-helix | 231-237 | 7 | |
| α-helix | 244-258 | 15 | |
| 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 | |
| α-helix | 440-442 | 3 | |
| β-strand | 448-449 | 2 | 1 |
Chain E: 22 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 762 | 1 | 3 |
| β-strand | 769 | 1 | 4 |
| α-helix | 772-774 | 3 | |
| α-helix | 780-783 | 4 | |
| α-helix | 794-802 | 9 | |
| β-strand | 803 | 1 | 3 |
| β-strand | 831 | 1 | 5 |
| 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 | |
| β-strand | 900 | 1 | 5 |
| α-helix | 902-910 | 9 | |
| α-helix | 916-927 | 12 | |
| α-helix | 929-952 | 24 | |
| α-helix | 954-970 | 17 | |
| β-strand | 981-982 | 2 | 6 |
| α-helix | 984-992 | 9 | |
| β-strand | 994 | 1 | 7 |
| β-strand | 1001 | 1 | 7 |
| α-helix | 1002-1013 | 12 | |
| α-helix | 1015-1019 | 5 | |
| α-helix | 1020-1023 | 4 | |
| α-helix | 1027-1032 | 6 | |
| α-helix | 1035-1057 | 23 | |
| α-helix | 1059-1061 | 3 | |
| α-helix | 1069-1104 | 36 | |
| α-helix | 1114-1167 | 54 | |
| α-helix | 1181-1191 | 11 | |
Chain F: 23 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 752-754 | 3 | |
| β-strand | 762 | 1 | 14 |
| β-strand | 769 | 1 | 12 |
| α-helix | 772-774 | 3 | |
| α-helix | 780-783 | 4 | |
| α-helix | 794-801 | 8 | |
| β-strand | 803 | 1 | 14 |
| α-helix | 839-850 | 12 | |
| α-helix | 854-863 | 10 | |
| α-helix | 871-879 | 9 | |
| α-helix | 882-883 | 2 | |
| α-helix | 884-888 | 5 | |
| α-helix | 902-910 | 9 | |
| α-helix | 916-927 | 12 | |
| α-helix | 937-952 | 16 | |
| α-helix | 954-970 | 17 | |
| β-strand | 982 | 1 | 11 |
| α-helix | 984-992 | 9 | |
| β-strand | 994 | 1 | 15 |
| β-strand | 1001 | 1 | 15 |
| α-helix | 1002-1013 | 12 | |
| α-helix | 1017-1019 | 3 | |
| α-helix | 1020-1023 | 4 | |
| α-helix | 1027-1031 | 5 | |
| α-helix | 1035-1057 | 23 | |
| α-helix | 1059-1061 | 3 | |
| α-helix | 1069-1104 | 36 | |
| α-helix | 1114-1167 | 54 | |
| α-helix | 1181-1191 | 11 | |
Chain G: 27 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 753-756 | 4 | |
| β-strand | 762 | 1 | 10 |
| β-strand | 769 | 1 | 11 |
| α-helix | 772-774 | 3 | |
| α-helix | 780-783 | 4 | |
| α-helix | 788-790 | 3 | |
| α-helix | 795-801 | 7 | |
| β-strand | 803 | 1 | 10 |
| α-helix | 839-850 | 12 | |
| α-helix | 854-863 | 10 | |
| α-helix | 871-880 | 10 | |
| α-helix | 882-883 | 2 | |
| α-helix | 884-890 | 7 | |
| α-helix | 891-899 | 9 | |
| α-helix | 902-909 | 8 | |
| α-helix | 916-933 | 18 | |
| α-helix | 937-952 | 16 | |
| α-helix | 954-970 | 17 | |
| β-strand | 982 | 1 | 12 |
| α-helix | 984-988 | 5 | |
| α-helix | 990-992 | 3 | |
| β-strand | 994 | 1 | 13 |
| β-strand | 1001 | 1 | 13 |
| 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 | 1059-1061 | 3 | |
| α-helix | 1069-1104 | 36 | |
| α-helix | 1114-1169 | 56 | |
| α-helix | 1181-1190 | 10 | |
| α-helix | 1193-1195 | 3 | |
Chain H: 23 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 752-756 | 5 | |
| β-strand | 762 | 1 | 8 |
| β-strand | 769-770 | 2 | 6 |
| α-helix | 772-774 | 3 | |
| α-helix | 780-783 | 4 | |
| α-helix | 794-801 | 8 | |
| β-strand | 803 | 1 | 8 |
| α-helix | 837-850 | 14 | |
| α-helix | 854-863 | 10 | |
| α-helix | 871-880 | 10 | |
| α-helix | 882-883 | 2 | |
| α-helix | 884-890 | 7 | |
| α-helix | 894-899 | 6 | |
| α-helix | 902-911 | 10 | |
| α-helix | 916-952 | 37 | |
| α-helix | 954-970 | 17 | |
| β-strand | 982 | 1 | 4 |
| α-helix | 984-989 | 6 | |
| β-strand | 994 | 1 | 9 |
| β-strand | 1001 | 1 | 9 |
| α-helix | 1002-1012 | 11 | |
| α-helix | 1015-1019 | 5 | |
| α-helix | 1020-1023 | 4 | |
| α-helix | 1027-1031 | 5 | |
| α-helix | 1035-1055 | 21 | |
| α-helix | 1059-1062 | 4 | |
| α-helix | 1069-1104 | 36 | |
| α-helix | 1114-1166 | 53 | |
| α-helix | 1182-1189 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein diaphanous homolog 1 | A, B, C, D | protein | 330 | Mus musculus | O08808 (AlphaFold model) |
| Protein diaphanous homolog 1 | E, F, G, H | protein | 467 | Mus musculus | O08808 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>3O4X_1 Protein diaphanous homolog 1 (chains A, B, C, D)
GSESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKR
LHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMI
DAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQL
INALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLK
GRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEEC
VSQIVLHKNGTDPDFKCRHLQIDIERLVDQ
Sequence of entity 2 (E, F, G, H), FASTA
>3O4X_2 Protein diaphanous homolog 1 (chains E, F, G, H)
GSFGFGVPAAPVLPFGLTPKKVYKPEVQLRRPNWSKFVAEDLSQDCFWTKVKEDRFENNE
LFAKLTLAFSAQTKTSKAKKDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMP
YQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMGTV
PRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAG
SRNAGAFGFNISFLCKLRDTKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRV
SAENLQKSLDQMKKQIADVERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSN
METLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKE
KAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRG
Primary citation
Crystal structure of a complex between amino and carboxy terminal fragments of mDia1: insights into autoinhibition of diaphanous-related formins. Nezami, A., Poy, F., Toms, A. et al. PLoS One (2010) 5:e12992-e12992. DOI 10.1371/journal.pone.0012992 · 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
- 3OBV 2.75 Å, Autoinhibited Formin mDia1 Structure
- 1Z2C 3.0 Å, Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP
- 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
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