9ZZJ: One Lmod2 at the pointed end of F-actin
One Lmod2 at the pointed end of F-actin. Determined by electron microscopy at 3.28 Å resolution. Released 24 Jun 2026.
- Method
- Electron microscopy
- Resolution
- 3.28 Å
- Organisms
- Oryctolagus cuniculus, Homo sapiens
- Chains
- 6
- Atoms
- 15,875
- Mol. weight
- 274.5 kDa
- Ligands
- ADP, MG
- Released
- 24 Jun 2026
Explore 9ZZJ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9ZZJ contains 122 α-helices and 102 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: 24 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-7 | 2 | |
| β-strand | 8-11 | 4 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-37 | 3 | 2 |
| α-helix | 59-61 | 3 | |
| β-strand | 66-68 | 3 | 2 |
| β-strand | 72 | 1 | 3 |
| β-strand | 75 | 1 | 3 |
| 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 | 137-145 | 9 | |
| β-strand | 149-155 | 7 | 4 |
| β-strand | 160-166 | 7 | 4 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 4 |
| α-helix | 182-194 | 13 | |
| α-helix | 203-205 | 3 | |
| α-helix | 206-215 | 10 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-242 | 5 | 5 |
| β-strand | 246-250 | 5 | 5 |
| α-helix | 252-254 | 3 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-266 | 3 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 4 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 4 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-347 | 10 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-369 | 4 | |
Chain B: 25 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-12 | 5 | 6 |
| β-strand | 16-21 | 6 | 6 |
| β-strand | 29-32 | 4 | 6 |
| β-strand | 35-37 | 3 | 7 |
| α-helix | 45-47 | 3 | |
| β-strand | 53-54 | 2 | 7 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 66-68 | 3 | 7 |
| β-strand | 71-72 | 2 | 8 |
| β-strand | 75-76 | 2 | 8 |
| α-helix | 80-88 | 9 | |
| α-helix | 89-93 | 5 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 6 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 6 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-155 | 6 | 9 |
| β-strand | 160-166 | 7 | 9 |
| β-strand | 169-170 | 2 | 9 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 9 |
| α-helix | 182-193 | 12 | |
| α-helix | 194-196 | 3 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238 | 1 | 10 |
| β-strand | 241 | 1 | 11 |
| β-strand | 247 | 1 | 11 |
| β-strand | 250 | 1 | 10 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-266 | 3 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 9 |
| α-helix | 303-305 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 9 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-346 | 9 | |
| β-strand | 357-358 | 2 | 6 |
| α-helix | 359-364 | 6 | |
| α-helix | 369-373 | 5 | |
Chain C: 21 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| 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 | 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 | 14 |
| β-strand | 75-76 | 2 | 14 |
| α-helix | 80-91 | 12 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 12 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 12 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-155 | 6 | 15 |
| β-strand | 160-166 | 7 | 15 |
| β-strand | 169-170 | 2 | 15 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 15 |
| α-helix | 182-193 | 12 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 16 |
| β-strand | 247-250 | 4 | 16 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-266 | 3 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 15 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 15 |
| α-helix | 338-347 | 10 | |
| α-helix | 350-352 | 3 | |
| β-strand | 357-358 | 2 | 12 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 | |
Chain D: 24 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-12 | 5 | 17 |
| β-strand | 16-21 | 6 | 17 |
| β-strand | 29-32 | 4 | 17 |
| β-strand | 35-38 | 4 | 18 |
| β-strand | 42 | 1 | 9 |
| β-strand | 53-54 | 2 | 18 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 18 |
| β-strand | 71-72 | 2 | 19 |
| β-strand | 75-76 | 2 | 19 |
| α-helix | 80-87 | 8 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 17 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 17 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-155 | 6 | 20 |
| β-strand | 160-166 | 7 | 20 |
| β-strand | 169-170 | 2 | 20 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 20 |
| α-helix | 182-193 | 12 | |
| α-helix | 194-196 | 3 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 21 |
| β-strand | 247-250 | 4 | 21 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| 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 | 20 |
| α-helix | 303-305 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 20 |
| α-helix | 338-347 | 10 | |
| α-helix | 353-355 | 3 | |
| β-strand | 357-358 | 2 | 17 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 | |
Chain E: 22 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-12 | 5 | 22 |
| β-strand | 16-21 | 6 | 22 |
| β-strand | 29-32 | 4 | 22 |
| β-strand | 35-38 | 4 | 23 |
| β-strand | 42 | 1 | 15 |
| β-strand | 53-54 | 2 | 23 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 23 |
| β-strand | 71-72 | 2 | 24 |
| β-strand | 75-76 | 2 | 24 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 22 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 22 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-155 | 6 | 25 |
| β-strand | 160-166 | 7 | 25 |
| β-strand | 169-170 | 2 | 25 |
| β-strand | 176-178 | 3 | 25 |
| α-helix | 182-193 | 12 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 26 |
| β-strand | 247-250 | 4 | 26 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-266 | 3 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-301 | 5 | 25 |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 25 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-347 | 10 | |
| α-helix | 351-354 | 4 | |
| β-strand | 357-358 | 2 | 22 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 | |
Chain L: 6 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 199-207 | 9 | |
| β-strand | 215-217 | 3 | 27 |
| α-helix | 226-236 | 11 | |
| β-strand | 244-246 | 3 | 27 |
| α-helix | 254-266 | 13 | |
| β-strand | 272-274 | 3 | 27 |
| α-helix | 282-291 | 10 | |
| β-strand | 300-302 | 3 | 27 |
| α-helix | 312-322 | 11 | |
| β-strand | 330-332 | 3 | 27 |
| α-helix | 338-362 | 25 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Actin, alpha skeletal muscle | A, B, C, D, E | protein | 375 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Leiomodin-2 | L | protein | 556 | Homo sapiens | Q6P5Q4 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E), FASTA
>9ZZJ_1 Actin, alpha skeletal muscle (chains A, B, C, D, E)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF
Sequence of entity 2 (L), FASTA
>9ZZJ_2 Leiomodin-2 (chains L)
MHHHHHHSGMSTFGYRRGLSKYESIDEDELLASLSAEELKELERELEDIEPDRNLPVGLR
QKSLTEKTPTGTFSREALMAYWEKESQKLLEKERLGECGKVAEDKEESEEELIFTESNSE
VSEEVYTEEEEEESQEEEEEEDSDEEERTIETAKGINGTVNYDSVNSDNSKPKIFKSQIE
NINLTNGSNGRNTESPAAIHPCGNPTVIEDALDKIKSNDPDTTEVNLNNIENITTQTLTR
FAEALKDNTVVKTFSLANTHADDSAAMAIAEMLKVNEHITNVNVESNFITGKGILAIMRA
LQHNTVLTELRFHNQRHIMGSQVEMEIVKLLKENTTLLRLGYHFELPGPRMSMTSILTRN
MDKQRQKRLQEQKQQEGYDGGPNLRTKVWQRGTPSSSPYVSPRHSPWSSPKLPKKVQTVR
SRPLSPVATPPPPPPPPPPPPPSSQRLPPPPPPPPPPLPEKKLITRNIAEVIKQQESAQR
ALQNGQKKKKGKKVKKQPNSILKEIKNSLRSVQEKKMEDSSRPSTPQRSAHENLMEAIRG
SSIKQLKRVEVPEALR
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 5 |
| MG | Magnesium ion | Mg | 5 |
Primary citation
Mechanism of actin thin filament pointed-end elongation by leiomodin. Brotzman, S.B., Palmer, N.J., Boczkowska, M. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-74810-6 · 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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