1G88: S4AFL3ARG515 mutant

S4AFL3ARG515 mutant. Determined by X-ray diffraction at 3.0 Å resolution. Released 29 Nov 2000.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 3
Atoms: 5,431
Mol. weight: 88.04 kDa
Released: 29 Nov 2000

Explore 1G88 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1G88 contains 27 α-helices and 43 β-strands across 3 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, 13 β-strands

Element	Residues	Length	Sheet
β-strand	288-291	4	1
α-helix	318-320	3
β-strand	322-330	9	1
β-strand	333-334	2	1
α-helix	337-338	2
β-strand	339-342	4	1
β-strand	347-351	5	2
β-strand	361-363	3	2
α-helix	374-380	7
β-strand	387-392	6	2
β-strand	396-401	6	2
β-strand	407-410	4	1
α-helix	412-417	6
β-strand	426-429	4	1
α-helix	430	1
β-strand	434-438	5	2
α-helix	440-456	17
α-helix	492-495	4
α-helix	496-499	4
β-strand	500-505	6	1
α-helix	518-520	3
β-strand	524-529	6	1
α-helix	530-539	10

Chain B: 9 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	288-291	4	3
α-helix	318-320	3
β-strand	322-330	9	3
β-strand	333-334	2	3
α-helix	337-338	2
β-strand	339-342	4	3
β-strand	347-351	5	4
β-strand	361-363	3	4
α-helix	374-383	10
β-strand	387-392	6	4
β-strand	396-401	6	4
β-strand	407-410	4	3
α-helix	412-417	6
β-strand	426-429	4	3
β-strand	434-438	5	4
α-helix	440-465	26
β-strand	484	1	5
α-helix	492-495	4
α-helix	496-499	4
β-strand	500-504	5	3
α-helix	518-520	3
β-strand	524-529	6	3
α-helix	530-540	11
β-strand	549	1	5

Chain C: 8 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	288-291	4	6
α-helix	318-320	3
β-strand	322-330	9	6
β-strand	333-334	2	6
α-helix	337-338	2
β-strand	339-342	4	6
β-strand	347-351	5	7
β-strand	361-363	3	7
α-helix	374-381	8
β-strand	387-392	6	7
β-strand	396-401	6	7
β-strand	407-410	4	6
α-helix	412-417	6
β-strand	426-429	4	6
β-strand	434-438	5	7
α-helix	440-462	23
β-strand	484	1	8
α-helix	492-497	6
β-strand	500-504	5	6
α-helix	518-520	3
β-strand	524-529	6	6
α-helix	530-540	11
β-strand	549	1	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
SMAD4	A, B, C	protein	268	Homo sapiens	Q13485 (AlphaFold model)

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

>1G88_1 SMAD4 (chains A, B, C)
NGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSS
CPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSD
HAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAA
VAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPSQSIKETPCW
IEIHLHRALQLLDEVLHTMPIADPQPLD

Primary citation

The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization. Chacko, B.M., Qin, B., Correia, J.J. et al. Nat Struct Biol (2001) 8:248-253. DOI 10.1038/84995 · PubMed

Other PDB entries of the same protein (UniProt Q13485 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6YIC 1.6 Å, 14-3-3 sigma in complex with SMAD4 pS403 peptide
9HWE 1.7 Å, SMAD4 MH2, residues 314-552
9HZA 2.03 Å, SMAD4 MH2, residues 272-552
5MEY 2.05 Å, Crystal structure of Smad4-MH1 bound to the GGCGC site.
1YGS 2.1 Å, Crystal structure of the SMAD4 tumor suppressor C-terminal domain
9QE6 2.1 Å, SMAD4 MH2 domain (residues 314-552) bound by Nanobody A1 (NbA1)
5UWU 2.24 Å, Crystal Structure of SMAD4 NES Peptide in complex with CRM1-Ran-RanBP1
1U7F 2.6 Å, Crystal Structure of the phosphorylated Smad3/Smad4 heterotrimeric complex
5C4V 2.6 Å, Ski-like protein
1DD1 2.62 Å, Crystal structure analysis of the SMAD4 active fragment
1U7V 2.7 Å, Crystal Structure of the phosphorylated Smad2/Smad4 heterotrimeric complex
1MR1 2.85 Å, Crystal Structure of a Smad4-Ski Complex

Browse structure collections

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