1OZO: Apo-S100P protein determined by NMR spectroscopy

Three-dimensional solution structure of apo-S100P protein determined by NMR spectroscopy. Determined by solution NMR. Released 20 Apr 2004.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 1,456
Mol. weight: 20.79 kDa
Released: 20 Apr 2004

Explore 1OZO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1OZO contains 12 α-helices and 4 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: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-18	16
β-strand	27-29	3	1
α-helix	30-40	11
α-helix	44-46	3
α-helix	56-62	7
β-strand	68-70	3	1
α-helix	71-85	15

Chain B: 7 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-17	15
β-strand	28-29	2	2
α-helix	30-33	4
α-helix	37-40	4
α-helix	44-46	3
α-helix	56-59	4
α-helix	62-64	3
β-strand	68-69	2	2
α-helix	71-85	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
S-100P protein	A, B	protein	95	Homo sapiens	P25815 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1OZO_1 S-100P protein (chains A, B)
MTELEAAMGMIIDVFSRYSGSEGSTQTLTKGELKVLMEKELPGFLQSGKDKDAVDKLLKD
LDANGDAQVDFSEFIVFVAAITSASHKYFEKTGLK

Primary citation

NMR structure of the Apo-S100P protein. Lee, Y.-C., Volk, D.E., Thiviyanathan, V. et al. J Biomol NMR (2004) 29:399-402. DOI 10.1023/B:JNMR.0000032617.88899.4b · PubMed

Other PDB entries of the same protein (UniProt P25815 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1J55 2.0 Å, The Crystal Structure of Ca+-bound Human S100P Determined at 2.0A Resolution by X-ray
7NMI 2.1 Å, Transactivation domain of p53 in complex with S100P, using annexin A2 as crystallization…
2MJW Structural Insights into Calcium Bound S100P - V Domain of the receptor for advanced…

Browse structure collections

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