Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution. Determined by X-ray diffraction at 1.75 Å resolution. Released 2 May 2001.
Explore 1D4X in 3D Show helices and sheets RCSB PDB PDBe
1D4X contains 32 α-helices and 28 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-7 | 3 | |
| β-strand | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 22 | 1 | 2 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 3 |
| β-strand | 53-54 | 2 | 3 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 3 |
| β-strand | 71-72 | 2 | 4 |
| β-strand | 75-76 | 2 | 4 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-94 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 5 |
| β-strand | 160-166 | 7 | 5 |
| β-strand | 169-170 | 2 | 5 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 5 |
| α-helix | 182-194 | 13 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 253-262 | 10 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| α-helix | 326-327 | 2 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 338-348 | 11 | |
| α-helix | 350-352 | 3 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-369 | 3 | |
| α-helix | 370-373 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-10 | 5 | |
| β-strand | 16-23 | 8 | 7 |
| β-strand | 26-29 | 4 | 7 |
| α-helix | 30-31 | 2 | |
| α-helix | 32-34 | 3 | |
| β-strand | 37-39 | 3 | 8 |
| β-strand | 43-51 | 9 | 7 |
| β-strand | 57-65 | 9 | 7 |
| α-helix | 71-87 | 17 | |
| β-strand | 92-98 | 7 | 7 |
| α-helix | 104-107 | 4 | |
| β-strand | 115-117 | 3 | 8 |
| α-helix | 121-123 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| C. Elegans actin 1/3 | A | protein | 375 | Caenorhabditis elegans | P0DM41 (AlphaFold model) |
| Gelsolin | G | protein | 126 | Homo sapiens | P06396 (AlphaFold model) |
>1D4X_1 C. ELEGANS ACTIN 1/3 (chains A) CDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT QIMFETFNTPAMYVAIQAVLSLYASGRTTGVVLDSGDGVTHTVPIYEGYALPHAILRLDL AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY ELPDGQVITVGNERFRCPEAMFQPSFLGMESAGIHETSYNSIMKCDIDIRKDLYANTVLS GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ EYDESGPSIVHRKCF
>1D4X_2 GELSOLIN (chains G) MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYD LHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG VASGFK
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
| SO2 | Sulfur dioxide | O2 S | 1 |
| CA | Calcium ion | Ca | 1 |
Water and common crystallization additives (SO4) are not listed.
The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism. Vorobiev, S., Strokopytov, B., Drubin, D.G. et al. Proc Natl Acad Sci U S A (2003) 100:5760-5765. DOI 10.1073/pnas.0832273100 · PubMed
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