6RSQ: Helical folded domain of mouse CAP1

Helical folded domain of mouse CAP1. Determined by X-ray diffraction at 2.37 Å resolution. Released 27 Nov 2019.

Method: X-ray diffraction
Resolution: 2.37 Å
Organism: Mus musculus
Chains: 4
Atoms: 5,698
Mol. weight: 90.02 kDa
Released: 27 Nov 2019

Explore 6RSQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6RSQ contains 35 α-helices and 2 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: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	38-40	3
α-helix	41-64	24
α-helix	66-91	26
β-strand	93	1	1
α-helix	94-95	2
α-helix	98-119	22
α-helix	127-134	8
α-helix	137-144	8
α-helix	149-171	23
α-helix	177-199	23
α-helix	204-206	3
β-strand	207	1	1

Chain B: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	38-40	3
α-helix	41-64	24
α-helix	66-91	26
α-helix	98-120	23
α-helix	127-134	8
α-helix	137-144	8
α-helix	149-171	23
α-helix	177-199	23

Chain C: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	35-39	5
α-helix	41-64	24
α-helix	66-91	26
α-helix	93-96	4
α-helix	100-120	21
α-helix	127-134	8
α-helix	137-144	8
α-helix	149-171	23
α-helix	176-199	24

Chain D: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	41-64	24
α-helix	66-91	26
α-helix	93-96	4
α-helix	99-120	22
α-helix	127-134	8
α-helix	137-144	8
α-helix	149-171	23
α-helix	176-199	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Adenylyl cyclase-associated protein 1	A, B, C, D	protein	198	Mus musculus	P40124 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>6RSQ_1 Adenylyl cyclase-associated protein 1 (chains A, B, C, D)
MKHHHHHHHHHHSAGLEVLFQGPYVQAFDSLLANPVAEYLKMSKEIGGDVQKHAEMVHTG
LKLERALLATASQCQQPAGNKLSDLLAPISEQIQEVITFREKNRGSKFFNHLSAVSESIQ
ALGWVALAAKPGPFVKEMNDAAMFYTNRVLKEYRDVDKKHVDWVRAYLSIWTELQAYIKE
FHTTGLAWSKTGPVAKEL

Primary citation

Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin. Kotila, T., Wioland, H., Enkavi, G. et al. Nat Commun (2019) 10:5320-5320. DOI 10.1038/s41467-019-13213-2 · PubMed

Other PDB entries of the same protein (UniProt P40124 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6RSW 1.95 Å, HFD domain of mouse CAP1 bound to the pointed end of G-actin
6FM2 2.8 Å, CARP domain of mouse cyclase-associated protein 1 (CAP1) bound to ADP-actin

Browse structure collections

About this viewer

MolViewer shows 6RSQ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.