9ZF4: PDB entry 9ZF4

The structure of human Vacuolar Protein Sorting 34 catalytic domain bound to RD-II-83. Determined by X-ray diffraction at 2.09 Å resolution. Released 22 Apr 2026.

Method
X-ray diffraction
Resolution
2.09 Å
Organism
Homo sapiens
Chains
1
Atoms
4,555
Mol. weight
69.32 kDa
Ligands
MG, A1C15
Released
22 Apr 2026

Explore 9ZF4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9ZF4 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 A: 34 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-helix360-3667
α-helix374-38512
α-helix389-40214
α-helix403-4053
α-helix408-4136
α-helix444-4474
α-helix475-48511
α-helix487-50216
α-helix504-5096
α-helix511-53020
α-helix533-56129
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-strand672-67651
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-helix793-81119
α-helix813-8219
α-helix829-8324
α-helix835-84511
α-helix852-86918

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Phosphatidylinositol 3-kinase catalytic subunit type 3Aprotein594Homo sapiensQ8NEB9 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9ZF4_1 Phosphatidylinositol 3-kinase catalytic subunit type 3 (chains A)
MGHHHHHHHHHHAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCV
NWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLL
QLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPP
PASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMY
LNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALL
GDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKH
GDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTE
GSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKL
FHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLIL
NLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALF

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2
A1C15methyl 2-[(8R)-pyrazolo[1,5-a]pyrimidin-3-yl]-1,3-benzothiazole-6-carboxylateC15 H10 N4 O2 S1

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

Primary citation

The structure of human Vacuolar Protein Sorting 34 catalytic domain bound to RD-II-83. Litchfield, C.M., Abiodun, W.O., Burtch, M. 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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