7NXV: Complex of DNase I/G-actin/PPP1R15A_582-621
Crystal structure of the complex of DNase I/G-actin/PPP1R15A_582-621. Determined by X-ray diffraction at 2.55 Å resolution. Released 29 Sept 2021.
- Method
- X-ray diffraction
- Resolution
- 2.55 Å
- Organisms
- Oryctolagus cuniculus, Bos taurus, Homo sapiens
- Chains
- 6
- Atoms
- 10,650
- Mol. weight
- 153.54 kDa
- Ligands
- CA, ATP
- Released
- 29 Sept 2021
Explore 7NXV in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7NXV contains 79 α-helices and 78 β-strands across 6 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: 25 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7 | 1 | |
| 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 | 42-44 | 3 | 4 |
| α-helix | 48-50 | 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 | 5 |
| β-strand | 75-76 | 2 | 5 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-93 | 5 | |
| 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 | 6 |
| β-strand | 160-166 | 7 | 6 |
| β-strand | 169-170 | 2 | 6 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 6 |
| α-helix | 182-195 | 14 | |
| α-helix | 203-206 | 4 | |
| α-helix | 208-216 | 9 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 7 |
| β-strand | 247-250 | 4 | 7 |
| α-helix | 253-259 | 7 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 6 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 6 |
| α-helix | 338-346 | 9 | |
| α-helix | 351-354 | 4 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 | |
Chain B: 12 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-11 | 10 | 4 |
| α-helix | 13-17 | 5 | |
| α-helix | 19-29 | 11 | |
| β-strand | 34-40 | 7 | 4 |
| α-helix | 46-55 | 10 | |
| β-strand | 64-67 | 4 | 4 |
| α-helix | 68-70 | 3 | |
| β-strand | 71 | 1 | 8 |
| β-strand | 78 | 1 | 8 |
| β-strand | 79-84 | 6 | 4 |
| β-strand | 90-96 | 7 | 9 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-119 | 6 | 9 |
| β-strand | 127-132 | 6 | 9 |
| α-helix | 137-139 | 3 | |
| α-helix | 140-158 | 19 | |
| β-strand | 163-168 | 6 | 9 |
| α-helix | 178-183 | 6 | |
| α-helix | 185-188 | 4 | |
| β-strand | 192-194 | 3 | 9 |
| β-strand | 203 | 1 | 10 |
| β-strand | 212-217 | 6 | 9 |
| α-helix | 219-224 | 6 | |
| β-strand | 225 | 1 | 11 |
| β-strand | 231-232 | 2 | 4 |
| α-helix | 235-238 | 4 | |
| α-helix | 243-249 | 7 | |
| β-strand | 252 | 1 | 10 |
| β-strand | 255-258 | 4 | 4 |
| β-strand | 259 | 1 | 11 |
Chain C: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 583-602 | 20 | |
| α-helix | 604-606 | 3 | |
| α-helix | 609-618 | 10 | |
Chain D: 25 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-7 | 2 | |
| β-strand | 8-12 | 5 | 12 |
| β-strand | 16-21 | 6 | 12 |
| β-strand | 29-32 | 4 | 12 |
| β-strand | 35-38 | 4 | 13 |
| β-strand | 42-44 | 3 | 14 |
| α-helix | 48-50 | 3 | |
| β-strand | 53-54 | 2 | 13 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 13 |
| β-strand | 71-72 | 2 | 15 |
| β-strand | 75-76 | 2 | 15 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-93 | 5 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 12 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 12 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 16 |
| β-strand | 160-166 | 7 | 16 |
| β-strand | 169-170 | 2 | 16 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 16 |
| α-helix | 182-194 | 13 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-231 | 9 | |
| β-strand | 238-241 | 4 | 17 |
| β-strand | 247-250 | 4 | 17 |
| α-helix | 253-259 | 7 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 16 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 16 |
| α-helix | 338-346 | 9 | |
| α-helix | 350-354 | 5 | |
| β-strand | 357-358 | 2 | 12 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 | |
Chain E: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 584-603 | 20 | |
| α-helix | 604-607 | 4 | |
| α-helix | 609-619 | 11 | |
Chain F: 11 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-11 | 10 | 14 |
| α-helix | 13-17 | 5 | |
| α-helix | 19-30 | 12 | |
| β-strand | 34-40 | 7 | 14 |
| α-helix | 46-55 | 10 | |
| β-strand | 64-67 | 4 | 14 |
| α-helix | 68-70 | 3 | |
| β-strand | 71 | 1 | 18 |
| β-strand | 78 | 1 | 18 |
| β-strand | 79-84 | 6 | 14 |
| β-strand | 90-96 | 7 | 19 |
| β-strand | 114-119 | 6 | 19 |
| β-strand | 127-132 | 6 | 19 |
| α-helix | 137-139 | 3 | |
| α-helix | 140-158 | 19 | |
| β-strand | 163-168 | 6 | 19 |
| α-helix | 178-183 | 6 | |
| α-helix | 185-188 | 4 | |
| β-strand | 192-194 | 3 | 19 |
| β-strand | 203 | 1 | 20 |
| β-strand | 212-217 | 6 | 19 |
| α-helix | 219-224 | 6 | |
| β-strand | 225 | 1 | 21 |
| β-strand | 231-232 | 2 | 14 |
| α-helix | 235-238 | 4 | |
| α-helix | 243-249 | 7 | |
| β-strand | 252 | 1 | 20 |
| β-strand | 255-258 | 4 | 14 |
| β-strand | 259 | 1 | 21 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Actin, alpha skeletal muscle, intermediate form | A, D | protein | 375 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Deoxyribonuclease-1 | B, F | protein | 260 | Bos taurus | P00639 (AlphaFold model) |
| Protein phosphatase 1 regulatory subunit 15A | C, E | protein | 40 | Homo sapiens | O75807 (AlphaFold model) |
Sequence of entity 1 (A, D), FASTA
>7NXV_1 Actin, alpha skeletal muscle, intermediate form (chains A, D)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF
Sequence of entity 2 (B, F), FASTA
>7NXV_2 Deoxyribonuclease-1 (chains B, F)
LKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDP
NTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSS
HSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQ
WSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYG
LSNEMALAISDHYPVEVTLT
Sequence of entity 3 (C, E), FASTA
>7NXV_3 Protein phosphatase 1 regulatory subunit 15A (chains C, E)
WEQLARDRSRFARRITQAQEELSPCLTPAARARAWARLRN
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CA | Calcium ion | Ca | 6 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 2 |
Primary citation
Higher-order phosphatase-substrate contacts terminate the integrated stress response. Yan, Y., Harding, H.P., Ron, D. Nat Struct Mol Biol (2021) 28:835-846. DOI 10.1038/s41594-021-00666-7 · PubMed
Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4B1Y 1.29 Å, Structure of the Phactr1 RPEL-3 bound to G-actin
- 2FXU 1.35 Å, X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
- 4K41 1.4 Å, Crystal structure of actin in complex with marine macrolide kabiramide C
- 1QZ5 1.45 Å, Structure of rabbit actin in complex with kabiramide C
- 1WUA 1.45 Å, The structure of Aplyronine A-actin complex
- 2Q0U 1.45 Å, Structure of Pectenotoxin-2 and Latrunculin B Bound to Actin
- 2V52 1.45 Å, Structure of MAL-RPEL2 complexed to G-actin
- 3MN5 1.5 Å, Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation
- 2PBD 1.5 Å, Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*
- 5ZZA 1.53 Å, OdinProfilin/Rabbit Actin Complex
- 1J6Z 1.54 Å, Uncomplexed actin
- 1QZ6 1.6 Å, Structure of rabbit actin in complex with jaspisamide A
Browse structure collections
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