8V1L: NTF2L domain of human G3BP1

Crystal structure of the NTF2L domain of human G3BP1 in complex with small molecule. Determined by X-ray diffraction at 2.68 Å resolution. Released 14 Feb 2024.

Method
X-ray diffraction
Resolution
2.68 Å
Organism
Homo sapiens
Chains
6
Atoms
6,490
Mol. weight
99.68 kDa
Ligands
Y9M
Released
14 Feb 2024

Explore 8V1L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8V1L contains 31 α-helices and 44 β-strands across 6 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: 5 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix8-2417
α-helix27-337
β-strand34-4181
β-strand55-5621
α-helix57-6711
β-strand7412
β-strand77-8591
α-helix86-883
β-strand89-9791
β-strand9912
β-strand107-116101
β-strand124-133101
α-helix134-1363
Chain B: 5 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix8-2215
α-helix27-337
β-strand3413
β-strand39-4024
β-strand4113
β-strand4515
β-strand5115
α-helix52-543
β-strand55-5624
α-helix57-6610
β-strand74-85123
α-helix86-883
β-strand89-99113
β-strand106-116113
β-strand124-133103
Chain C: 5 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix8-2518
α-helix30-334
β-strand3416
β-strand39-4026
α-helix52-543
β-strand55-5626
α-helix58-6710
β-strand75-85116
β-strand89-98106
β-strand106-116116
β-strand124-133106
α-helix134-1374
Chain D: 4 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix8-2518
α-helix27-337
β-strand3417
β-strand39-4137
α-helix53-542
β-strand55-5627
α-helix57-6711
β-strand74-85127
β-strand89-99117
β-strand106-116117
β-strand124-133107
Chain E: 7 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix8-2518
α-helix27-293
α-helix31-333
β-strand39-4248
α-helix51-533
β-strand55-5628
α-helix57-6610
β-strand74-84118
α-helix86-883
β-strand90-99108
α-helix104-1052
β-strand106-116118
β-strand124-133108
Chain F: 5 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix8-2518
α-helix27-293
α-helix31-333
β-strand39-4139
α-helix53-542
β-strand55-5629
α-helix58-669
β-strand74-85129
β-strand89-99119
β-strand106-116119
β-strand124-133109

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ras GTPase-activating protein-binding protein 1A, B, C, D, E, Fprotein139Homo sapiensQ13283 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>8V1L_1 Ras GTPase-activating protein-binding protein 1 (chains A, B, C, D, E, F)
MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKE
IHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSV
ANKFYVHNDIFRYQDEVFG

Ligands and cofactors

IDNameFormulaCopies
Y9MN-[(2S)-2-fluoro-4,4-dimethylpentanoyl]-3-hydroxy-L-valyl-(betaS)-beta-methyl-L…C38 H56 F N5 O76

Primary citation

Identification of small molecule inhibitors of G3BP-driven stress granule formation. Freibaum, B.D., Messing, J., Nakamura, H. et al. J Cell Biol (2024) 223. DOI 10.1083/jcb.202308083 · PubMed

Other PDB entries of the same protein (UniProt Q13283 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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