9ZJQ: Human KLK3 following acylation by CDD-3290

Human KLK3 following acylation by CDD-3290. Determined by X-ray diffraction at 2.2 Å resolution. Released 24 Dec 2025.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
1
Atoms
1,948
Mol. weight
28.19 kDa
Ligands
A1C2U
Released
24 Dec 2025

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

Secondary structure: helices and β-sheets

9ZJQ contains 8 α-helices and 19 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: 8 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand2611
β-strand29-3022
β-strand39-4463
β-strand47-56103
β-strand59-6243
α-helix64-663
β-strand71-7553
β-strand7914
β-strand88-97103
α-helix103-1053
β-strand122-12653
α-helix129-1324
β-strand13315
β-strand13615
α-helix138-1425
α-helix145-1473
β-strand151-15662
β-strand17014
β-strand172-17982
α-helix181-1877
β-strand196-20052
β-strand20711
β-strand216-21942
β-strand222-22982
β-strand241-24552
α-helix246-2494
α-helix250-25910

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Prostate-specific antigenAprotein249Homo sapiensP07288 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9ZJQ_1 Prostate-specific antigen (chains A)
IVGGWECEKHSQPWQVLVASRGRAVCGGVLVHPQWVLTAAHCIRNKSVILLGRHSLFHPE
DTGQVFQVSHSFPHPLYDMSLLKNRFLRPGDDSSHDLMLLRLSEPAELTDAVKVMDLPTQ
EPALGTTCYASGWGSIEPEEFLTPKKLQCVDLHVISNDVCAQVHPQKVTKFMLCAGRWTG
GKSTCSGDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRKWIKDTIVANPEFV
EHHHHHHHH

Ligands and cofactors

IDNameFormulaCopies
A1C2U1H-1,3-benzimidazole-5-carbaldehydeC8 H6 N2 O1

Water and common crystallization additives (EDO) are not listed.

Primary citation

Human KLK3 following acylation by CDD-3290. Fraser, B.J., Dong, A., Wilson, R. et al. To be published.

Other PDB entries of the same protein (UniProt P07288 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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