4B1V: Phactr1 RPEL-N domain

Structure of the Phactr1 RPEL-N domain bound to G-actin. Determined by X-ray diffraction at 1.75 Å resolution. Released 7 Nov 2012.

Method
X-ray diffraction
Resolution
1.75 Å
Organisms
ORYCTOLAGUS CUNICULUS, MUS MUSCULUS
Chains
4
Atoms
6,803
Mol. weight
93.9 kDa
Ligands
ATP, LAB, MG
Released
7 Nov 2012

Explore 4B1V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4B1V contains 54 α-helices and 38 β-strands across 4 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, 19 β-strands

ElementResiduesLengthSheet
β-strand8-1251
β-strand16-2161
β-strand29-3241
β-strand35-3622
β-strand53-5422
α-helix56-594
β-strand67-6822
β-strand71-7223
β-strand75-7623
α-helix79-8810
α-helix89-946
α-helix98-1003
β-strand103-10751
α-helix113-1219
α-helix122-1265
β-strand131-13661
α-helix137-1448
β-strand150-15564
β-strand160-16674
β-strand169-17024
α-helix172-1743
β-strand176-17834
α-helix182-19312
α-helix194-1963
α-helix203-21614
α-helix223-23210
β-strand238-24145
β-strand247-25045
α-helix253-2597
α-helix264-2674
α-helix274-28310
α-helix287-2948
β-strand297-30044
α-helix302-3043
α-helix309-32012
α-helix325-3273
β-strand329-33024
α-helix335-3373
α-helix338-34710
α-helix350-3523
β-strand357-35821
α-helix359-3657
α-helix369-3735
Chain B: 24 helices, 19 β-strands
ElementResiduesLengthSheet
α-helix6-72
β-strand8-1256
β-strand16-2166
β-strand29-3246
β-strand35-3737
β-strand53-5427
α-helix56-594
β-strand66-6837
β-strand71-7228
β-strand75-7628
α-helix79-879
α-helix88-947
α-helix98-1003
β-strand103-10756
α-helix113-12513
β-strand131-13666
α-helix137-1448
β-strand150-15569
β-strand160-16679
β-strand169-17029
α-helix172-1743
β-strand176-17839
α-helix182-19312
α-helix194-1963
α-helix203-21614
α-helix223-23210
β-strand238-241410
β-strand247-250410
α-helix253-2597
α-helix264-2674
α-helix274-28310
α-helix287-2948
β-strand297-30049
α-helix302-3054
α-helix309-32012
α-helix325-3273
β-strand329-33029
α-helix335-3373
α-helix338-34710
α-helix350-3523
β-strand357-35826
α-helix359-3657
α-helix369-3735
Chains M and N: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix138-1458
α-helix147-1493
α-helix150-1556

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha skeletal muscleA, Bprotein376ORYCTOLAGUS CUNICULUSP68135 (AlphaFold model)
Phosphatase and actin regulator 1M, Nprotein32MUS MUSCULUSQ2M3X8 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4B1V_1 ACTIN, ALPHA SKELETAL MUSCLE (chains A, B)
CDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKM
TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLD
LAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKS
YELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVM
SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITK
QEYDEAGPSIVHRKCF
Sequence of entity 2 (M, N), FASTA
>4B1V_2 PHOSPHATASE AND ACTIN REGULATOR 1 (chains M, N)
FKHTSAALERKISMRQSREELIKRGVLKEIYD

Ligands and cofactors

IDNameFormulaCopies
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P32
LABLatrunculin BC20 H29 N O5 S2
MGMagnesium ionMg2

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

Primary citation

Structures of the Phactr1 RPEL domain and RPEL motif complexes with G-actin reveal the molecular basis for actin binding cooperativity. Mouilleron, S., Wiezlak, M., O'Reilly, N. et al. Structure (2012) 20:1960-1970. DOI 10.1016/j.str.2012.08.031 · PubMed

Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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