Actin-DNAse I Complex. Determined by X-ray diffraction at 1.85 Å resolution. Released 1 Nov 2005.
Explore 2A42 in 3D Show helices and sheets RCSB PDB PDBe
2A42 contains 36 α-helices and 38 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 | 6-7 | 2 | |
| β-strand | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 2 |
| β-strand | 42-44 | 3 | 3 |
| α-helix | 48-50 | 3 | |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 2 |
| 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 | 113-125 | 13 | |
| 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 | 182-196 | 15 | |
| α-helix | 206-216 | 11 | |
| 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 | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-347 | 10 | |
| α-helix | 350-354 | 5 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-364 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-11 | 10 | 3 |
| α-helix | 13-16 | 4 | |
| α-helix | 19-29 | 11 | |
| β-strand | 34-40 | 7 | 3 |
| α-helix | 46-55 | 10 | |
| β-strand | 64-67 | 4 | 3 |
| α-helix | 68-70 | 3 | |
| β-strand | 71 | 1 | 7 |
| β-strand | 78 | 1 | 7 |
| β-strand | 79-84 | 6 | 3 |
| β-strand | 89-96 | 8 | 8 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-120 | 7 | 8 |
| β-strand | 127-132 | 6 | 8 |
| α-helix | 137-139 | 3 | |
| α-helix | 140-158 | 19 | |
| β-strand | 163-168 | 6 | 8 |
| α-helix | 178-183 | 6 | |
| α-helix | 185-188 | 4 | |
| β-strand | 192-194 | 3 | 8 |
| β-strand | 203 | 1 | 9 |
| β-strand | 212-217 | 6 | 8 |
| α-helix | 219-224 | 6 | |
| β-strand | 225 | 1 | 10 |
| α-helix | 226 | 1 | |
| β-strand | 231-232 | 2 | 3 |
| α-helix | 235-238 | 4 | |
| α-helix | 243-249 | 7 | |
| β-strand | 252 | 1 | 9 |
| β-strand | 255-258 | 4 | 3 |
| β-strand | 259 | 1 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | A | protein | 375 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Deoxyribonuclease-1 | B | protein | 260 | Bos taurus | P00639 (AlphaFold model) |
>2A42_1 Actin, alpha skeletal muscle (chains A) DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ EYDEAGPSIVHRKCF
>2A42_2 Deoxyribonuclease-1 (chains B) LKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDP NTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSS HSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQ WSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYG LSNEMALAISDHYPVEVTLT
Water and common crystallization additives (GOL) are not listed.
Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Chereau, D., Kerff, F., Graceffa, P. et al. Proc Natl Acad Sci U S A (2005) 102:16644-16649. DOI 10.1073/pnas.0507021102 · PubMed
Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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