9DKP: PDB entry 9DKP

The structure of human vacuolar protein sorting 34 catalytic domain bound to RD-I-53. Determined by X-ray diffraction at 2.16 Å resolution. Released 17 Sept 2025.

Method
X-ray diffraction
Resolution
2.16 Å
Organism
Homo sapiens
Chains
1
Atoms
4,274
Mol. weight
69.3 kDa
Ligands
ETZ, A1A6F, ETX
Released
17 Sept 2025

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

Secondary structure: helices and β-sheets

9DKP contains 34 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 B: 34 helices, 12 β-strands

ElementResiduesLengthSheet
α-helix293-3008
α-helix306-3094
α-helix310-3189
α-helix320-3223
α-helix327-3293
α-helix330-3356
α-helix342-35413
α-helix356-3594
α-helix360-3634
α-helix364-3674
α-helix374-38411
α-helix389-40214
α-helix403-4053
α-helix408-4136
α-helix475-48410
α-helix487-50216
α-helix504-5096
α-helix511-52919
α-helix533-55927
α-helix566-57813
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-helix690-6978
α-helix700-7078
β-strand70913
α-helix714-7163
β-strand71713
α-helix719-73820
β-strand749-75132
β-strand757-75932
α-helix781-7866
α-helix793-81119
α-helix813-8219
α-helix829-8324
α-helix835-8373
α-helix838-8469
α-helix852-87019

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Phosphatidylinositol 3-kinase catalytic subunit type 3Bprotein594Homo sapiensQ8NEB9 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>9DKP_1 Phosphatidylinositol 3-kinase catalytic subunit type 3 (chains B)
MGHHHHHHHHHHAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCV
NWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLL
QLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPP
PASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMY
LNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALL
GDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKH
GDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTE
GSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKL
FHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLIL
NLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALF

Ligands and cofactors

IDNameFormulaCopies
ETZdiethyl etherC4 H10 O2
A1A6F(8R)-3-(1,3-benzothiazol-2-yl)pyrazolo[1,5-a]pyrimidineC13 H8 N4 S1
ETX2-ethoxyethanolC4 H10 O21

Water and common crystallization additives (DMS, K, CL) are not listed.

Primary citation

Facile Bacterial Production of Human Vacuolar Protein Sorting 34 Enables Structural Characterization of Novel Inhibitors. Abiodun, W.O., Dass, R., Tsubaki, E. 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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