9VWT: Plasma kallikrein light chain

The catalytic domain of human plasma kallikrein with peptide inhibitor 070. Determined by X-ray diffraction at 1.77 Å resolution. Released 6 Aug 2025.

Method
X-ray diffraction
Resolution
1.77 Å
Organisms
Homo sapiens, synthetic construct
Chains
2
Atoms
2,073
Mol. weight
27.94 kDa
Released
6 Aug 2025

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

Secondary structure: helices and β-sheets

9VWT contains 12 α-helices and 25 β-strands across 2 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: 12 helices, 24 β-strands

ElementResiduesLengthSheet
β-strand1711
β-strand20-2122
α-helix22-232
β-strand30-3673
β-strand38B-48113
β-strand51-5443
α-helix56-594
α-helix62-65C3
β-strand65D-6743
β-strand7214
α-helix73-753
β-strand8313
β-strand85-9063
β-strand9515
β-strand10015
β-strand104-10853
α-helix111-1144
β-strand11516
β-strand11816
α-helix120-1212
β-strand12212
α-helix123-1253
α-helix126-1305
β-strand136-14052
β-strand15414
α-helix1551
β-strand156-15942
β-strand162-16322
α-helix165-1706
β-strand180-18342
β-strand18911
β-strand198-20362
β-strand208B-215102
β-strand226-23052
α-helix231-2344
α-helix235-2417
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand512

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Plasma kallikrein light chainAprotein237Homo sapiensP03952 (AlphaFold model)
peptide inhibitorBprotein10synthetic construct
Sequence of entity 1 (A), FASTA
>9VWT_1 Plasma kallikrein light chain (chains A)
IVGGTNSSWGEWPWQVSLQVKLTAQRHLCGGSLIGHQWVLTAAHCFDGLPLQDVWRIYSG
ILNLSDITKDTPFSQIKEIIIHQNYKVSEGNHDIALIKLQAPLNYTEFQKPISLPSKGDT
STIYTNCWVTGWGFSKEKGEIQNILQKVNIPLVTNEECQKRYQDYKITQRMVCAGYKEGG
KDACKGDSGGPLVCKHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWILEKTQS
Sequence of entity 2 (B), FASTA
>9VWT_2 peptide inhibitor (chains B)
CPAYSXYLDC

Primary citation

Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue. Lin, H., Xu, M., Jiang, L. et al. Bioorg Chem (2024) 152:107734-107734. DOI 10.1016/j.bioorg.2024.107734 · PubMed

Other PDB entries of the same protein (UniProt P03952 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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