9GLQ: P73 tetramerisation domain

Crystal structure of p73 tetramerisation domain in complex with darpins 1800. Determined by X-ray diffraction at 2.1 Å resolution. Released 22 Jan 2025.

Method
X-ray diffraction
Resolution
2.1 Å
Organisms
Homo sapiens, synthetic construct
Chains
3
Atoms
1,752
Mol. weight
25.49 kDa
Ligands
CO
Released
22 Jan 2025

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

Secondary structure: helices and β-sheets

9GLQ contains 13 α-helices and 0 β-strands across 3 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: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix362-37817
α-helix383-39614
Chain B: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix362-37716
α-helix378-3803
α-helix383-39311
Chain C: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix3-1412
α-helix17-259
α-helix40-467
α-helix50-589
α-helix73-808
α-helix83-919
α-helix106-1138
α-helix116-12510

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tumor protein p73A, Bprotein50Homo sapiensO15350 (AlphaFold model)
Darpins 1800Cprotein126synthetic construct
Sequence of entity 1 (A, B), FASTA
>9GLQ_1 Tumor protein p73 (chains A, B)
GSDEDTYYLQVRGRKNFEILMKLKESLELMELVPQPLVDSYRQQQQLLQR
Sequence of entity 2 (C), FASTA
>9GLQ_2 Darpins 1800 (chains C)
GSDLGKKLLEAAAVGQDDEVRILMANGADVNAMDQNGETPLHLAAMNGHLEIVEVLLKTG
ADVNASDFHGDTPLHLAAMAGHLEIVEVLLKHGADVNAQDTWGYIPFDLAAWAGNEDIAE
VLQKAA

Ligands and cofactors

IDNameFormulaCopies
COCobalt (II) ionCo1

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

Primary citation

DARPins as a novel tool to detect and degrade p73. Munick, P., Zielinski, J., Strubel, A. et al. Cell Death Dis (2024) 15:909-909. DOI 10.1038/s41419-024-07304-2 · PubMed

Other PDB entries of the same protein (UniProt O15350 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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