6JBK: Actin monomer
Crystal structure of an actin monomer in complex with the nucleator Cordon-Bleu WH2-motif peptide mutant. T22V. Determined by X-ray diffraction at 2.45 Å resolution. Released 5 Feb 2020.
- Method
- X-ray diffraction
- Resolution
- 2.45 Å
- Organisms
- Oryctolagus cuniculus, Mus musculus
- Chains
- 8
- Atoms
- 12,277
- Mol. weight
- 180.44 kDa
- Ligands
- CA, ATP
- Released
- 5 Feb 2020
Explore 6JBK in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6JBK contains 103 α-helices and 85 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: 22 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35 | 1 | 3 |
| β-strand | 54 | 1 | 3 |
| α-helix | 56-60 | 5 | |
| β-strand | 68 | 1 | 3 |
| β-strand | 71-72 | 2 | 4 |
| β-strand | 75-76 | 2 | 4 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 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 | 182-195 | 14 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 253-259 | 7 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| 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 | 338-348 | 11 | |
| α-helix | 350-355 | 6 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-371 | 5 | |
Chain B: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 67-78 | 12 | |
| α-helix | 80-83 | 4 | |
| β-strand | 85 | 1 | 2 |
| α-helix | 86 | 1 | |
Chain C: 23 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-12 | 5 | 7 |
| β-strand | 16-21 | 6 | 7 |
| β-strand | 24 | 1 | 8 |
| β-strand | 29-32 | 4 | 7 |
| β-strand | 35 | 1 | 9 |
| β-strand | 54 | 1 | 9 |
| α-helix | 56-60 | 5 | |
| β-strand | 68 | 1 | 9 |
| β-strand | 71-72 | 2 | 10 |
| β-strand | 75-76 | 2 | 10 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 7 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131-136 | 6 | 7 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 11 |
| β-strand | 160-166 | 7 | 11 |
| β-strand | 169-170 | 2 | 11 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 11 |
| α-helix | 182-196 | 15 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 12 |
| β-strand | 247-250 | 4 | 12 |
| α-helix | 253-262 | 10 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 11 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 11 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| α-helix | 350-355 | 6 | |
| β-strand | 357-358 | 2 | 7 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-371 | 5 | |
Chains D and H: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 67-77 | 11 | |
| α-helix | 80-83 | 4 | |
| β-strand | 85 | 1 | 8 |
| α-helix | 86 | 1 | |
Chain E: 23 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-7 | 2 | |
| β-strand | 8-12 | 5 | 13 |
| β-strand | 16-21 | 6 | 13 |
| β-strand | 22 | 1 | 14 |
| β-strand | 24 | 1 | 14 |
| β-strand | 29-32 | 4 | 13 |
| β-strand | 35 | 1 | 15 |
| β-strand | 54 | 1 | 15 |
| α-helix | 56-60 | 5 | |
| β-strand | 68 | 1 | 15 |
| β-strand | 71-72 | 2 | 16 |
| β-strand | 75-76 | 2 | 16 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 13 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 13 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 17 |
| β-strand | 160-166 | 7 | 17 |
| β-strand | 169-170 | 2 | 17 |
| β-strand | 176-178 | 3 | 17 |
| α-helix | 182-194 | 13 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 18 |
| β-strand | 247-250 | 4 | 18 |
| α-helix | 253-262 | 10 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 17 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 17 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| α-helix | 350-352 | 3 | |
| α-helix | 356 | 1 | |
| β-strand | 357-358 | 2 | 13 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-371 | 5 | |
Chain F: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 67-76 | 10 | |
| α-helix | 80-83 | 4 | |
| β-strand | 85 | 1 | 14 |
Chain G: 24 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-12 | 5 | 19 |
| β-strand | 16-21 | 6 | 19 |
| β-strand | 24 | 1 | 20 |
| β-strand | 29-32 | 4 | 19 |
| β-strand | 35 | 1 | 21 |
| β-strand | 54 | 1 | 21 |
| α-helix | 56-60 | 5 | |
| β-strand | 68 | 1 | 21 |
| β-strand | 71-72 | 2 | 22 |
| β-strand | 75-76 | 2 | 22 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 19 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131-136 | 6 | 19 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 23 |
| β-strand | 160-166 | 7 | 23 |
| β-strand | 169-170 | 2 | 23 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 23 |
| α-helix | 182-196 | 15 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 24 |
| β-strand | 247-250 | 4 | 24 |
| α-helix | 253-256 | 4 | |
| α-helix | 259-262 | 4 | |
| 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 | 23 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 23 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| α-helix | 350-355 | 6 | |
| β-strand | 357-358 | 2 | 19 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-371 | 5 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Actin, alpha skeletal muscle | A, C, E, G | protein | 377 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Peptide from Protein cordon-bleu | B, D, F, H | protein | 22 | Mus musculus | Q5NBX1 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>6JBK_1 Actin, alpha skeletal muscle (chains A, C, E, G)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF
Sequence of entity 2 (B, D, F, H), FASTA
>6JBK_2 Peptide from Protein cordon-bleu (chains B, D, F, H)
SLHSALMEAIHSSGGREKLRKV
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CA | Calcium ion | Ca | 8 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 4 |
Primary citation
Design of an actin-severing peptide. Scipion, C.P.M., Robinson, R.C. To be published.
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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