CODSWALLOP

Actin, alpha skeletal muscle

Homo sapiens · seed P68133 · 377 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026

CATH and SCOP identifiers come from the RCSB's own structure annotations, which the Domains panel already reads, so these are looked up rather than guessed at.

749Entries 866Entities 144Constructs 39Organisms 747Ligand-bound
1.15 ÅBest res.
3.29 ÅMedian res.

Every figure here is counted over the whole family rather than quoted from one entry.

The reference structure

2FXU, the structure every other member of this family is superposed onto. Rendered by the RCSB and embedded here: the live app shows an interactive viewport, which a document that fetches nothing cannot.

Rendered structure of 2FXU
2FXU at the RCSB · open it in the 3D viewer

Which residues anyone has ever seen

How many of this family's constructs contain each residue of the seed. A trough is a stretch nobody has put in a construct, which is a construct-design answer rather than a disorder one.

1188377866 constructs

Constructs, most-used first

144 distinct constructs across 749 entries. 418 polymer entities differ from the UniProt canonical sequence in some way, 13 carry a recognised expression tag and 0 carry a fusion partner.

"Differs from canonical" is not the same as "engineered". The canonical sequence is the full gene product, so a secreted protein whose structures all start after its signal peptide counts every one of them as different: lysozyme's most-used construct, residues 19–147 on 1,239 entities, is simply the mature protein. Read the construct column below for what was actually done, rather than this count.

EntitiesLengthBest (Å)Best entryWhat was made
160 375 1.35 2FXU residues 3-377
155 377 1.15 7W4Z matches the canonical sequence
78 375 2.40 3U4L matches the canonical sequence
46 377 2.79 9ZBL matches the canonical sequence
32 418 2.00 1K8K matches the canonical sequence
29 394 2.00 1K8K matches the canonical sequence
26 429 2.40 8QR1 matches the canonical sequence
24 376 3.30 7Z8I 2 internal deletions; W310F, S311G, R319D +25 more
17 371 1.90 2GWJ residues 7-377
16 376 1.29 4B1Y residues 2-377
15 374 2.18 9QEW residues 2-375; C272A
12 373 1.53 5ZZA residues 5-377
12 375 1.90 1YAG matches the canonical sequence
11 375 2.60 8K6V matches the canonical sequence
9 374 1.80 2HF3 residues 3-376; A205E, P244K
9 769 2.70 8OOP residues 98-866
8 374 2.20 3UB5 residues 2-375
7 378 1.22 6I4E matches the canonical sequence
6 373 4.60 6BNP residues 1-373
6 427 2.70 8UXW matches the canonical sequence
5 390 2.70 8UXW matches the canonical sequence
4 370 1.72 36OQ residues 7-376
4 370 3.02 8ZBN residues 7-376
3 367 8.00 5NOL residues 7-373; M301L, T360S
3 371 3.08 8ZI9 residues 7-377

Showing the 25 most-used of 144.

Positions people deliberately mutate

Columns where the wild-type residue still dominates but a real minority carries something else, which is a different question from "what varies across species".

M301L 50% E4D 46% T105V 44% N164T 44% T262A 44% T8A 44% L18M 44% T7I 44% N299I 44% A367S 43% I78V 43% T360S 42% N227Q 41% V203T 40% C12V 39% M178L 39% Y281F 36% I269L 36% D5E 34% A274C 34% E6D 33% V19C 32% V131T 31% I289V 30% D3M 30% L155M 28% A297G 25% A230K 24% M271V 24% T196R 24%

What it assembles into

Oligomeric stateChainsEntriesShare
dimeric2 150 20.0%
heptameric7 67 8.9%
tetrameric4 61 8.1%
pentameric5 60 8.0%
trimeric3 46 6.1%
decameric10 40 5.3%
octameric8 34 4.5%
monomeric1 33 4.4%

353 entries have the depositor's assembly corroborated by PISA, 387 carry the depositor's word alone and 8 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 17 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1D4X, 1NLV, 1NM1, 1NMD, 1P8Z, 1YAG, 1YVN, 2A40, 2Q97, 2YJF, 3CI5, 3CIP, 3M6G, 4V0U, 6DEC, 6WK1, 6WK2.

Domain architecture

Every source's own domains on the seed axis, one row each. They are not merged: Pfam, CATH, SCOP and InterPro disagree about boundaries, and a merged track would state a consensus none of them gave.

CATHSeverinActin; Chain A, domain 2ATPase, nucleotide bindingATPase, substrate binding SCOP2BActin-like ATPasesActin-like ATPasesActin-like ATPasesActin-like ATPasesActin-like ATPasesActin-like ATPasesActin-like ATPasesActin-like ATPasesActin-like ATPasesActin-like ATPasesActin-like ATPasesActin-like ATPasesActin-like ATPasesActin-like ATPasesActin-like ATPases1188377
DomainSourceSpan (seed)Chains
SeverinCATH 3.40.20.10 3–129 11
Actin; Chain A, domain 2CATH 2.30.36.70 37–70 67
ATPase, nucleotide binding domainCATH 3.30.420.40 145–187 837
ATPase, substrate binding domain, subdomain 4CATH 3.90.640.10 184–273 236
Actin-like ATPasesSCOP2B 8040506 7–148 243
Actin-like ATPasesSCOP2B 8043436 7–146 53
Actin-like ATPasesSCOP2B 8082531 7–149 14
Actin-like ATPasesSCOP2B 8044481 7–149 8
Actin-like ATPasesSCOP2B 8003798 8–149 8
Actin-like ATPasesSCOP2B 8037889 11–168 28
Actin-like ATPasesSCOP2B 8082549 11–153 13
Actin-like ATPasesSCOP2B 8043438 147–374 53

What binds it

ADP ADP420 entries ATP ATP247 entries ANP ANP30 entries LAB LAB28 entries LAR LAR18 entries 9UE 9UE12 entries GDP GDP10 entries GTP GTP7 entries AGS AGS7 entries AR6 AR66 entries SAH SAH5 entries NAD NAD4 entries
ComponentClassNameEntriesBest (Å)
ADPcofactor Adenosine-5'-Diphosphate 420 1.15
MGion Magnesium Ion 418 1.15
ATPcofactor Adenosine-5'-Triphosphate 247 1.24
CAion Calcium Ion 211 1.15
PO4ion Phosphate Ion 57 1.15
EDOcryoprotectant 1,2-Ethanediol 31 1.15
ANPcofactor Phosphoaminophosphonic Acid-Adenylate Ester 30 1.15
LABligand Latrunculin B 28 1.29
ZNion Zinc Ion 28 3.20
GOLcryoprotectant Glycerol 24 1.29
SO4ion Sulfate Ion 20 1.60
LARligand Latrunculin A 18 1.75
9UEligand Jasplakinolide 12 2.60
SCNion Thiocyanate Ion 11 1.22
GDPcofactor Guanosine-5'-Diphosphate 10 3.10
CLion Chloride Ion 9 1.24
BEFion Beryllium Trifluoride Ion 8 2.17
PEGcryoprotectant Di(Hydroxyethyl)ether 8 1.22
GTPcofactor Guanosine-5'-Triphosphate 7 3.10
AGScofactor Phosphothiophosphoric Acid-Adenylate Ester 7 2.75

How it crystallises

Parsed from the free text 218 depositors typed into _exptl_crystal_grow.pdbx_details, out of 222 entries that recorded anything at all. Median pH 6.6 (range 3.5 to 10.0).

Precipitants

PEG × Calcium chloride × Sodium chloride × Magnesium chloride × Ammonium sulfate × Lithium sulfate × Dioxane × MPD × Sodium formate × Sodium citrate × Tacsimate × Ethanol × Sodium malonate × Isopropanol ×

Buffers

HEPES × MES × Tris × Sodium acetate × Bis-Tris × Citrate × Sodium cacodylate × Bis-Tris propane × Imidazole × CAPS × Phosphate × CHES ×

Which entries to trust

736 entries carry a wwPDB validation report: 468 clean, 145 worth a check and 123 with something to explain. Median clashscore 6.13, median RSRZ outliers 2.95%, median R-free minus R-work 0.04. 712 have released structure factors.

Across species

OrganismEntriesBest (Å)Ligand-boundSeed covered
Oryctolagus cuniculus323 1.29 298 100%
Homo sapiens124 1.35 121 100%
Sus scrofa64 3.00 65 100%
Bos taurus41 2.00 60 100%
Gallus gallus58 1.15 56 100%
Mus musculus34 3.00 30 100%
Drosophila melanogaster13 1.80 14 100%
Plasmodium falciparum 3D713 1.22 13 99%
Dictyostelium discoideum13 1.60 13 100%
Thermochaetoides thermophila11 2.70 10 99%
Saccharomyces cerevisiae S288C8 2.80 7 99%
Limulus polyphemus1 9.50 0 97%

Seed sequence

377 residues, numbered every ten. Every identity figure in this document is measured against this sequence.

active or binding site modified residue or glycosylation disulphide cysteine transmembrane or signal the 15 most-substituted positions

1MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
61QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
121MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
181DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
241SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
301MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIT
361KQEYDEAGPS IVHRKCF

Sites are UniProt's curated features where the seed is a UniProt accession; the substituted positions are measured from this family's own alignment rather than annotated, and only the fifteen most substituted are marked: every position carrying a minority substitution would be most of the protein, because the family holds orthologues. A residue can carry more than one and is drawn with the first that applies, in the order of the key above.

Primary citations

One record per paper, not per entry.

YearCitation
2026 Mechanisms of disassembly at the actin filament pointed and barbed ends. Sci Adv doi:10.1126/sciadv.aee5882
2026 Mechanism of actin thin filament pointed-end elongation by leiomodin. Nat Commun doi:10.1038/s41467-026-74810-6
2026 Structural mechanisms of drebrin-mediated F-actin network modulation. Nat Commun doi:10.1038/s41467-026-74543-6
2026 Molecular basis of host ATP level modulation by actin-dependent secreted bacterial ATPase and its metaeffector. Nat Commun doi:10.1038/s41467-026-74513-y
2026 Structure and mechanism of an actin-dependent bacterial phosphoryl AMPylase. Nat.Chem.Biol. doi:10.1038/s41589-025-01945-w
2026 Structural basis for BCL7B-mediated ncBAF-nucleosome engagement. Nucleic Acids Res. doi:10.1093/nar/gkag092
2026 Evolutionarily conserved short linear motifs drive actin filament binding. Nat.Cell Biol. doi:10.1038/s41556-026-01979-9
2026 Tonotopic specialization of MYO7A isoforms in auditory hair cells. Nat Commun doi:10.1038/s41467-026-73220-y
2026 Actin arginylation alters myosin engagement and F-actin patterning despite structural conservation. J.Cell Biol. doi:10.1083/jcb.202409067
2026 The human BAF chromatin remodeler processes nucleosomes bound by pioneer transcription factors OCT4-SOX2. Mol.Cell doi:10.1016/j.molcel.2026.01.021
2026 Structural basis of human gamma TuRC closure during CM1-activated microtubule nucleation. Nat Commun doi:10.1038/s41467-026-70773-w
2026 Structural mechanism of histone H2A.Z exchange by human SRCAP-CFDP1 holoenzyme. Sci Adv doi:10.1126/sciadv.aei7728
2026 Roles of microtubules and LIS1 in dynein transport machinery assembly. Nature doi:10.1038/s41586-026-10153-y
2026 Leiomodin 2 is a processive pointed-end elongator of actin filaments. Nat Commun doi:10.1038/s41467-026-74809-z
2026 The structure of the native cardiac crossbridge in the rigor state. Sci Adv doi:10.1126/sciadv.aeg1209
2026 Structural basis of complex assembly and nucleosome recognition by the chromatin remodeling ncBAF complex. J Mol Cell Biol doi:10.1093/jmcb/mjag020
2026 Activation and regulation of the dynein-dynactin-NuMA complex. Nat.Chem.Biol. doi:10.1038/s41589-026-02156-7
2025 Microscopic and structural observations of actin filament capping and severing by cytochalasin D. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2502164122
2025 Choreography of rapid actin filament disassembly by coronin, cofilin, and AIP1. Cell doi:10.1016/j.cell.2025.09.016
2025 Aglycone Polyether Ionophores Affecting Actin Filaments as Broad-Spectrum Antiviral Agents. Acs Pharmacol Transl Sci doi:10.1021/acsptsci.5c00144
2025 Cryo-EM reconstruction of yeast ADP-actin filament at 2.5 angstrom resolution. A comparison with vertebrate F-actin. Structure doi:10.1016/j.str.2024.12.008
2025 Mechanism of actin filament severing and capping by gelsolin. Nat.Struct.Mol.Biol. doi:10.1038/s41594-024-01412-5
2025 The structure of an actin nucleus stabilized by villin. Sci Adv doi:10.1126/sciadv.adw6915
2025 High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2415457122
2025 Pseudo-acetylation of ACTC1 K326 and K328 promotes dysinhibition of reconstituted human cardiac thin filaments. J.Mol.Cell.Cardiol. doi:10.1016/j.yjmcc.2025.12.008
2025 Dimerization of GAS2 mediates crosslinking of microtubules and F-actin. Embo J. doi:10.1038/s44318-025-00415-2
2025 ncBAF recognizes the nucleosome through BCL7A in chromatin remodeling. Cell Discov doi:10.1038/s41421-025-00858-1
2025 NPF binding to Arp2 is allosterically linked to the release of ArpC5's N-terminal tail and conformational changes in Arp2/3 complex. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2421557122
2025 Biochemical and structural bases for talin ABSs-F-actin interactions. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2405922122
2025 Fascin structural plasticity mediates flexible actin bundle construction. Nat.Struct.Mol.Biol. doi:10.1038/s41594-024-01477-2
2025 Arp2/3-mediated bidirectional actin assembly by SPIN90 dimers. Nat.Struct.Mol.Biol. doi:10.1038/s41594-025-01665-8
2025 Actin isoform-specific interactions revealed by Vibrio VopV actin-binding repeats. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2523856122
2025 Harnessing the Evolution of Proteostasis Networks to Reverse Cognitive Dysfunction. Biorxiv doi:10.1101/2025.02.28.640897
2025 Trypanosome doublet microtubule structures reveal flagellum assembly and motility mechanisms. Science doi:10.1126/science.adr3314
2025 Structure of the F-tractin-F-actin complex. J.Cell Biol. doi:10.1083/jcb.202409192
2025 Unveiling the structural proteome of an Alzheimer's disease rat brain model. Structure doi:10.1016/j.str.2024.11.004
2025 Activation of Arp2/3 complex by a SPIN90 dimer in linear actin-filament nucleation. Nat.Struct.Mol.Biol. doi:10.1038/s41594-025-01673-8
2025 The Chlamydia effector Dre1 binds dynactin to reposition host organelles during infection. Cell Rep doi:10.1016/j.celrep.2025.115509
2025 The hypertrophic cardiomyopathy-associated A331P actin variant enhances basal contractile activity and elicits resting muscle dysfunction. Iscience doi:10.1016/j.isci.2025.111816
2025 Cryo-EM structure revealed a novel F-actin binding motif in a Legionella pneumophila lysine fatty-acyltransferase Elife doi:10.7554/elife.106975.1