3GXL: ALK-5 kinase complex with GW857175

ALK-5 kinase complex with GW857175. Determined by X-ray diffraction at 1.8 Å resolution. Released 21 Apr 2009.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
1
Atoms
2,460
Mol. weight
35.08 kDa
Ligands
QIG
Released
21 Apr 2009

Explore 3GXL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3GXL contains 16 α-helices and 16 β-strands across 1 chain. 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, 16 β-strands

ElementResiduesLengthSheet
α-helix2-43
β-strand6-1381
β-strand18-2361
β-strand29-3461
α-helix36-383
α-helix39-4911
β-strand5912
β-strand62-6981
β-strand74-8071
β-strand8712
α-helix88-947
β-strand9713
α-helix99-11719
β-strand12014
β-strand12614
β-strand128-13035
α-helix136-1383
β-strand139-14132
β-strand147-14932
β-strand156-15945
β-strand164-16525
α-helix176-1783
α-helix181-1844
α-helix193-21321
β-strand21513
α-helix222-2243
α-helix238-2425
α-helix243-2475
α-helix262-27211
α-helix279-2813
α-helix283-2842
α-helix285-29713

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
TGF-beta receptor type-1Aprotein303Homo sapiensP36897 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3GXL_1 TGF-beta receptor type-1 (chains A)
IARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENIL
GFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEI
VGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPNHRVGTKRYMA
PEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEE
MRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQQEG
IKM

Ligands and cofactors

IDNameFormulaCopies
QIGN-1H-indazol-5-yl-2-(6-methylpyridin-2-yl)quinazolin-4-amineC21 H16 N61

Primary citation

Design of novel quinazoline derivatives and related analogues as potent and selective ALK5 inhibitors. Gellibert, F., Fouchet, M.-H., Nguyen, V.-L. et al. Bioorg Med Chem Lett (2009) 19:2277-2281. DOI 10.1016/j.bmcl.2009.02.087 · PubMed

Other PDB entries of the same protein (UniProt P36897 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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