9RV5: SPSB2 SPRY domain

Crystal structure of SPSB2 SPRY domain in complex with linear TAT peptide. Determined by X-ray diffraction at 1.75 Å resolution. Released 6 Aug 2025.

Method
X-ray diffraction
Resolution
1.75 Å
Organism
Homo sapiens
Chains
4
Atoms
3,405
Mol. weight
52.82 kDa
Released
6 Aug 2025

Explore 9RV5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9RV5 contains 14 α-helices and 36 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.

Chains A and C: 7 helices, 18 β-strands

ElementResiduesLengthSheet
α-helix24-263
α-helix29-346
α-helix36-394
α-helix40-456
β-strand48-5361
β-strand57-6042
α-helix61-633
β-strand65-6842
β-strand75-8061
β-strand8413
β-strand88-9472
α-helix97-993
β-strand105-10951
β-strand116-11721
β-strand130-13451
β-strand13914
β-strand140-14121
α-helix149-1502
β-strand15114
β-strand166-17272
β-strand177-18262
β-strand185-19172
β-strand19913
β-strand200-20561
β-strand211-21882

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
SPRY domain-containing SOCS box protein 2A, Cprotein217Homo sapiensQ99619 (AlphaFold model)
Tat PeptideB, Dprotein20Homo sapiens
Sequence of entity 1 (A, C), FASTA
>9RV5_1 SPRY domain-containing SOCS box protein 2 (chains A, C)
MHHHHHHSSGVDLGTENLYFQSMPEGLEELLSAPPPDLGAQRRHGWNPKDCSENIEVKEG
GLYFERRPVAQSTDGARGKRGYSRGLHAWEISWPLEQRGTHAVVGVATALAPLQTDHYAA
LLGSNSESWGWDIGRGKLYHQSKGPGAPQYPAGTQGEQLEVPERLLVVLDMEEGTLGYAI
GGTYLGPAFRGLKGRTLYPAVSAVWGQCQVRIRYLGE
Sequence of entity 2 (B, D), FASTA
>9RV5_2 Tat Peptide (chains B, D)
YGRKKRRQRRRGSGVDINNN

Primary citation

Crystal structure of SPSB2 SPRY domain in complex with linear TAT peptide. Lenz, C., Knapp, S., Kraemer, A. et al. To be published.

Other PDB entries of the same protein (UniProt Q99619 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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