9D58: Dystrophin

Human Dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation. Determined by X-ray diffraction at 1.94 Å resolution. Released 12 Mar 2025.

Method: X-ray diffraction
Resolution: 1.94 Å
Organism: Homo sapiens
Chains: 4
Atoms: 7,475
Mol. weight: 114.29 kDa
Released: 12 Mar 2025

Explore 9D58 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9D58 contains 64 α-helices and 0 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: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	16-33	18
α-helix	36-39	4
α-helix	50-60	11
α-helix	65-68	4
α-helix	72-88	17
α-helix	98-102	5
α-helix	106-117	12
α-helix	118-124	7
α-helix	127-133	7
α-helix	138-149	12
α-helix	163-165	3
α-helix	169-178	10
α-helix	185-189	5
α-helix	194-207	14
α-helix	217-220	4
α-helix	227-240	14

Chain B: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	16-33	18
α-helix	36-39	4
α-helix	50-60	11
α-helix	65-67	3
α-helix	72-88	17
α-helix	98-102	5
α-helix	106-117	12
α-helix	118-124	7
α-helix	127-133	7
α-helix	138-149	12
α-helix	163-165	3
α-helix	169-178	10
α-helix	185-189	5
α-helix	194-207	14
α-helix	217-220	4
α-helix	227-240	14

Chain C: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	16-33	18
α-helix	36-39	4
α-helix	50-60	11
α-helix	65-68	4
α-helix	72-88	17
α-helix	98-102	5
α-helix	106-117	12
α-helix	118-124	7
α-helix	127-132	6
α-helix	138-149	12
α-helix	163-165	3
α-helix	169-178	10
α-helix	185-189	5
α-helix	194-207	14
α-helix	217-220	4
α-helix	227-240	14

Chain D: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	17-33	17
α-helix	36-39	4
α-helix	50-60	11
α-helix	65-67	3
α-helix	72-88	17
α-helix	98-102	5
α-helix	106-117	12
α-helix	118-124	7
α-helix	127-133	7
α-helix	138-149	12
α-helix	163-165	3
α-helix	169-178	10
α-helix	185-189	5
α-helix	194-207	14
α-helix	217-220	4
α-helix	227-240	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Dystrophin	A, B, C, D	protein	248	Homo sapiens	P11532 (AlphaFold model)

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

>9D58_1 Dystrophin (chains A, B, C, D)
STGLWWEEVEDSYEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLT
GQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHW
QVKNVMKNIMAGLQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRP
DLFDWNSVVSQQSATQRLEHAFNIARYQLGIEKLLDPEDVDTTYPDKKSILMYITSLFQV
LPQQVSIE

Primary citation

Human dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation. Streeter, O., Shi, K., Vavra, J. et al. Acta Crystallogr D Struct Biol (2025) 81:122-129. DOI 10.1107/S2059798325001457 · PubMed

Other PDB entries of the same protein (UniProt P11532 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1EG3 2.0 Å, Structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide
1EG4 2.0 Å, Structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide
9EC1 2.14 Å, The Structure of Human Dystrophin Spectrin Repeat 24
3UUN 2.3 Å, Crystal Structure of N-terminal first spectrin repeat of dystrophin
1DXX 2.6 Å, N-terminal Actin-binding Domain of Human Dystrophin

Browse structure collections

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