1MK2: SMAD3 SBD complex

Name: PDB 1MK2: SMAD3 SBD complex
Published: 2002-10-16
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transcription

SMAD3 SBD complex. Determined by X-ray diffraction at 2.74 Å resolution. Released 16 Oct 2002.

Method: X-ray diffraction
Resolution: 2.74 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,848
Mol. weight: 27.29 kDa
Released: 16 Oct 2002

Explore 1MK2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MK2 contains 12 α-helices and 15 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: 9 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	220-224	5	1
β-strand	232-238	7	2
β-strand	241-249	9	2
β-strand	253-257	5	3
β-strand	264	1	3
β-strand	267-269	3	3
α-helix	280-286	7
β-strand	293-298	6	3
β-strand	301-306	6	3
β-strand	312-315	4	2
α-helix	317-321	5
α-helix	322-324	3
α-helix	325-326	2
β-strand	331-333	3	2
β-strand	338-342	5	3
α-helix	344-355	12
α-helix	358-363	6
α-helix	364-369	6
β-strand	370-375	6	2
α-helix	388-390	3
β-strand	394-399	6	2
α-helix	400-413	14

Chain B: 3 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	677-679	3
β-strand	682	1	3
α-helix	686-691	6
α-helix	699-701	3
β-strand	702-706	5	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Smad 3	A	protein	206	Homo sapiens	P84022 (AlphaFold model)
Madh-interacting protein	B	protein	38	Homo sapiens	O95405 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1MK2_1 SMAD 3 (chains A)
DLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNR
NAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCN
LKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELH
LNGPLQWLDKVLTQMGSPSIRCSSVS

Sequence of entity 2 (B), FASTA

>1MK2_2 Madh-interacting protein (chains B)
SPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVG

Primary citation

Smad3 allostery links TGF-beta receptor kinase activation to transcriptional control. Qin, B.Y., Lam, S.S., Correia, J.J. et al. Genes Dev (2002) 16:1950-1963. DOI 10.1101/gad.1002002 · PubMed

Other PDB entries of the same protein (UniProt P84022 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6YIB 1.7 Å, 14-3-3 sigma in complex with SMAD3 pS423 peptide
1MJS 1.91 Å, MH2 domain of transcriptional factor SMAD3
5OD6 2.0 Å, Crystal structure of Smad3-MH1 bound to the GGCGC site.
5ODG 2.12 Å, Crystal structure of Smad3-MH1 bound to the GGCT site.
6ZMN 2.33 Å, Crystal structure of the Smad3-Smad5 MH1 domain chimera bound to the GGCGC site
1OZJ 2.4 Å, Crystal structure of Smad3-MH1 bound to DNA at 2.4 A resolution
5XOC 2.4 Å, Crystal structure of human Smad3-FoxH1 complex
1U7F 2.6 Å, Crystal Structure of the phosphorylated Smad3/Smad4 heterotrimeric complex
1MHD 2.8 Å, Crystal structure of a smad MH1 domain bound to DNA
2LAJ Third WW domain of human Nedd4L in complex with doubly phosphorylated human smad3…
2LB2 Structure of the second domain of human Nedd4L in complex with a phosphorylated pTPY…

Browse structure collections

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