9NIN: PDB entry 9NIN

The structure of human Vacuolar Protein Sorting 34 catalytic domain bound to RD-I-86. Determined by X-ray diffraction at 2.01 Å resolution. Released 4 Mar 2026.

Method
X-ray diffraction
Resolution
2.01 Å
Organism
Homo sapiens
Chains
1
Atoms
4,656
Mol. weight
69.43 kDa
Ligands
A1BYW
Released
4 Mar 2026

Explore 9NIN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9NIN contains 36 α-helices and 12 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: 36 helices, 12 β-strands

ElementResiduesLengthSheet
α-helix292-30110
α-helix306-3094
α-helix310-3189
α-helix320-3234
α-helix327-3293
α-helix330-3356
α-helix342-35413
α-helix356-3594
α-helix360-3634
α-helix364-3674
α-helix374-38512
α-helix389-40214
α-helix403-4053
α-helix408-4136
α-helix434-4374
α-helix475-48511
α-helix487-50216
α-helix504-5096
α-helix511-52919
α-helix533-56028
α-helix566-57813
α-helix580-5834
β-strand591-59331
β-strand596-60491
α-helix606-6083
β-strand610-61121
α-helix6181
β-strand619-62571
β-strand630-63781
α-helix642-66019
β-strand672-67431
β-strand679-68351
β-strand688-68922
α-helix690-6967
α-helix700-7078
β-strand70913
α-helix714-7163
β-strand71713
α-helix719-73820
β-strand749-75132
β-strand757-75932
α-helix781-7866
α-helix793-81018
α-helix813-82210
α-helix829-8324
α-helix835-8373
α-helix838-8469
α-helix852-86817

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Phosphatidylinositol 3-kinase catalytic subunit type 3Aprotein594Homo sapiensQ8NEB9 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9NIN_1 Phosphatidylinositol 3-kinase catalytic subunit type 3 (chains A)
MGHHHHHHHHHHAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCV
NWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLL
QLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPP
PASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMY
LNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALL
GDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKH
GDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTE
GSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKL
FHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLIL
NLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALF

Ligands and cofactors

IDNameFormulaCopies
A1BYW2-[(8R)-pyrazolo[1,5-a]pyrimidin-3-yl]-1,3-benzothiazol-6-olC13 H8 N4 O S1

Water and common crystallization additives (K, CL, PEG, EDO, ACT) are not listed.

Primary citation

The structure of human Vacuolar Protein Sorting 34 catalytic domain bound to RD-I-86. Abiodun, W.O., Dass, R., Singleton, J.D. et al. To be published.

Other PDB entries of the same protein (UniProt Q8NEB9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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