1KHU: SMAD1

Smad1 crystal structure reveals the details of BMP signaling pathway. Determined by X-ray diffraction at 2.5 Å resolution. Released 12 Dec 2001.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Homo sapiens
Chains
4
Atoms
6,772
Mol. weight
98.18 kDa
Released
12 Dec 2001

Explore 1KHU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KHU contains 32 α-helices and 50 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: 7 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand272-27871
β-strand281-28221
β-strand287-28821
β-strand293-29752
β-strand308-31032
α-helix321-3277
β-strand334-33852
β-strand342-34762
β-strand353-35641
α-helix358-3636
β-strand372-37431
β-strand379-38462
α-helix385-3939
α-helix400-4045
α-helix405-4106
β-strand411-41661
α-helix429-4313
β-strand435-44061
α-helix441-45111
Chain B: 9 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand272-27873
β-strand281-28223
α-helix285-2862
β-strand287-28823
β-strand293-29754
β-strand308-31034
α-helix321-3299
β-strand334-33964
β-strand342-34764
β-strand353-35643
α-helix358-3647
β-strand371-37443
β-strand379-38464
α-helix385-39511
α-helix396-3983
α-helix400-4045
α-helix405-4106
β-strand411-41663
β-strand42115
β-strand42715
α-helix429-4313
β-strand435-44063
α-helix441-45111
Chain C: 8 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand272-27876
β-strand281-28226
α-helix285-2862
β-strand287-28826
β-strand293-29647
β-strand30817
α-helix321-3277
β-strand334-33967
β-strand342-34767
β-strand353-35646
α-helix358-3647
β-strand372-37436
β-strand379-38467
α-helix385-39511
α-helix400-4056
α-helix408-4103
β-strand411-41666
α-helix429-4313
β-strand435-44066
α-helix441-45313
Chain D: 8 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand272-27878
β-strand281-28228
α-helix285-2862
β-strand287-28828
β-strand293-29759
β-strand308-31039
α-helix321-3277
β-strand334-33859
β-strand342-34769
β-strand353-35648
α-helix358-3647
β-strand372-37438
β-strand379-38469
α-helix385-39511
α-helix401-4044
α-helix405-4106
β-strand411-41668
α-helix429-4313
β-strand435-44068
α-helix441-45111

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
SMAD1A, B, C, Dprotein218Homo sapiensQ15797 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>1KHU_1 SMAD1 (chains A, B, C, D)
APPLPSEINRGDVQAVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKN
RFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFH
PTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFETVYELTKMCTIRMSFVKGWGAEYHRQ
DVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS

Primary citation

Structural basis of Smad1 activation by receptor kinase phosphorylation. Qin, B.Y., Chacko, B.M., Lam, S.S. et al. Mol Cell (2001) 8:1303-1312. DOI 10.1016/S1097-2765(01)00417-8 · PubMed

Other PDB entries of the same protein (UniProt Q15797 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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