7W51: Fragmin domain-1

Crystal structure of fragmin domain-1 in complex with actin (ADP-form). Determined by X-ray diffraction at 1.2 Å resolution. Released 26 Oct 2022.

Method
X-ray diffraction
Resolution
1.2 Å
Organisms
Gallus gallus, Physarum polycephalum
Chains
2
Atoms
5,278
Mol. weight
61.21 kDa
Ligands
CA, MG, ADP
Released
26 Oct 2022

Explore 7W51 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7W51 contains 34 α-helices and 30 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.

Chain A: 23 helices, 21 β-strands

ElementResiduesLengthSheet
β-strand8-1251
β-strand16-2161
β-strand2412
β-strand29-3241
β-strand35-3843
β-strand53-5423
α-helix55-606
α-helix62-643
β-strand65-6843
β-strand71-7224
β-strand75-7624
α-helix79-879
α-helix88-947
α-helix98-1003
β-strand103-10751
β-strand11215
α-helix113-12513
β-strand131-13661
α-helix137-1448
β-strand150-15566
β-strand160-16676
β-strand169-17026
α-helix172-1743
β-strand176-17836
α-helix182-19312
α-helix194-1963
α-helix203-21614
α-helix223-23210
β-strand238-24147
β-strand247-25047
α-helix253-26210
α-helix264-2674
α-helix274-28310
α-helix287-2948
β-strand297-30046
α-helix302-3054
α-helix309-32012
β-strand329-33026
α-helix335-3373
α-helix338-3469
α-helix350-3545
β-strand357-35821
α-helix359-3657
α-helix369-3735
Chain B: 11 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix9-113
β-strand1215
α-helix20-3011
α-helix34-363
β-strand44-5188
β-strand54-5748
α-helix58-592
α-helix60-623
β-strand65-6739
β-strand71-7888
β-strand88-9588
α-helix101-11717
α-helix1221
β-strand123-12868
α-helix134-1374
β-strand146-14839
α-helix152-1543
α-helix1561
β-strand15712
α-helix158-1592

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha skeletal muscleAprotein377Gallus gallusP68139 (AlphaFold model)
Actin-binding protein fragmin PBprotein162Physarum polycephalumQ94707 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>7W51_1 Actin, alpha skeletal muscle (chains A)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF
Sequence of entity 2 (B), FASTA
>7W51_2 Actin-binding protein fragmin P (chains B)
GPMQKQKEYNIADSNIANLGTELEKKVKLEASQHEDAWKGAGKQVGVEIWRIQQFKVVPV
PKKHHGSFYTGDSYIVLSTYHPKTNPDKLAYDVHFWLGAFTTQDEAGTAAYKTVELDDYL
GGLPVQYREVQGYESERFLSLFPKGGLRILDGGVETGFHHVE

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2
MGMagnesium ionMg1
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21

Water and common crystallization additives (EDO) are not listed.

Primary citation

Structures and mechanisms of actin ATP hydrolysis. Kanematsu, Y., Narita, A., Oda, T. et al. Proc Natl Acad Sci U S A (2022) 119:e2122641119-e2122641119. DOI 10.1073/pnas.2122641119 · PubMed

Other PDB entries of the same protein (UniProt P68139 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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