3UPV: TPR2B-domain:pHsp70-complex of yeast Sti1

TPR2B-domain:pHsp70-complex of yeast Sti1. Determined by X-ray diffraction at 1.6 Å resolution. Released 25 Jan 2012.

Method: X-ray diffraction
Resolution: 1.6 Å
Organisms: Saccharomyces cerevisiae, Saccharomyces cerevisiae S288c
Chains: 2
Atoms: 1,181
Mol. weight: 14.96 kDa
Released: 25 Jan 2012

Explore 3UPV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3UPV contains 8 α-helices and 0 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: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	260-274	15
α-helix	278-291	14
α-helix	296-308	13
α-helix	312-325	14
α-helix	330-342	13
α-helix	346-364	19
α-helix	369-382	14

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	651-653	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Heat shock protein STI1	A	protein	126	Saccharomyces cerevisiae	P15705 (AlphaFold model)
Heat shock protein SSA4	B	protein	7	Saccharomyces cerevisiae S288c	P22202 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3UPV_1 Heat shock protein STI1 (chains A)
SMKAEEARLEGKEYFTKSDWPNAVKAYTEMIKRAPEDARGYSNRAAALAKLMSFPEAIAD
CNKAIEKDPNFVRAYIRKATAQIAVKEYASALETLDAARTKDAEVNNGSSAREIDQLYYK
ASQQRF

Sequence of entity 2 (B), FASTA

>3UPV_2 Heat shock protein SSA4 (chains B)
PTVEEVD

Primary citation

The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. Schmid, A.B., Lagleder, S., Grawert, M.A. et al. EMBO J (2012) 31:1506-1517. DOI 10.1038/emboj.2011.472 · PubMed

Other PDB entries of the same protein (UniProt P15705 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3UQ3 2.6 Å, TPR2AB-domain:pHSP90-complex of yeast Sti1
2LLV Solution structure of the yeast Sti1 DP1 domain
2LLW Solution structure of the yeast Sti1 DP2 domain

Browse structure collections

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