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NMR structure of the histone-interacting N-terminal homodimeric region of Rtt106

Solution NMR
PDB entry 2lh0 coloured by chain, ensemble of 20 models, front view.
PDB entry 2lh0 coloured by chain, ensemble of 20 models, side view.
PDB entry 2lh0 coloured by chain, ensemble of 20 models, top view.
Source organism: Saccharomyces cerevisiae S288C
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Histone chaperone RTT106
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Multimeric state: homo dimer
Accessible surface area: 13781.16 Å2
Buried surface area: 1716.97 Å2
Dissociation area: 858.49 Å2
Dissociation energy (ΔGdiss): 11.93 kcal/mol
Dissociation entropy (TΔSdiss): 11.14 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-154040

Macromolecules

Histone chaperone RTT106
Chains: A, B
Length: 70 amino acids
Theoretical weight: 8.13 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P40161 (Residues: 1-67; Coverage: 15%)
Gene names: N1346, RTT106, YNL206C
Pfam: Histone chaperone Rtt106 N-terminal domain
InterPro:
CATH: RTT106-like
Histone chaperone RTT106 in PDB entry 2lh0, assembly 1, front view.
Histone chaperone RTT106 in PDB entry 2lh0, assembly 1, side view.
Histone chaperone RTT106 in PDB entry 2lh0, assembly 1, top view.
PDBe-KB: UniProt Coverage View: P40161  
170510152025303540455055606570
 
204060GHMMSKLFLDELPESLSRKIGTVVRVLPSSLEIFEELYKYALNENSNDRSEHHKKPRIDDSSDLLKTDEI
UniProt
P40161
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces
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