1ELW: TPR1 domain of HOP

Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide. Determined by X-ray diffraction at 1.6 Å resolution. Released 26 Apr 2000.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Homo sapiens
Chains
4
Atoms
2,240
Mol. weight
29.34 kDa
Ligands
NI
Released
26 Apr 2000

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

Secondary structure: helices and β-sheets

1ELW contains 16 α-helices and 0 β-strands across 4 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

ElementResiduesLengthSheet
α-helix3-1614
α-helix20-3314
α-helix38-5114
α-helix54-6714
α-helix72-8413
α-helix88-9912
α-helix106-11712
Chain B: 7 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix2-1615
α-helix20-3314
α-helix38-5114
α-helix54-6714
α-helix72-8413
α-helix88-10114
α-helix106-1149
Chains C and D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix9-113

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
TPR1-domain of hopA, Bprotein118Homo sapiensP31948 (AlphaFold model)
HSC70-peptideC, Dprotein8
Sequence of entity 1 (A, B), FASTA
>1ELW_1 TPR1-DOMAIN OF HOP (chains A, B)
MEQVNELKEKGNKALSVGNIDDALQCYSEAIKLDPHNHVLYSNRSAAYAKKGDYQKAYED
GCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLKHEANNPQLKEGLQNMEAR
Sequence of entity 2 (C, D), FASTA
>1ELW_2 HSC70-PEPTIDE (chains C, D)
GPTIEEVD

Ligands and cofactors

IDNameFormulaCopies
NINickel (II) ionNi4

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

Primary citation

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Scheufler, C., Brinker, A., Bourenkov, G. et al. Cell (2000) 101:199-210. DOI 10.1016/S0092-8674(00)80830-2 · PubMed

Other PDB entries of the same protein (UniProt P31948 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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