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RTT109 peptide bound to ASF1

Analyse RTT109 peptide bound to ASF1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6F0Y
Type: protein
Length: 187 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone chaperone ASF1; Histone acetyltransferase RTT109 C-terminus
EC: 2.3.1.48
UniProt: P32447

Structure

solution nmr · 2 distinct chains · 6% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone chaperone ASF1	protein	172	7% helix, 44% strand	P32447
B	Histone acetyltransferase RTT109 C-terminus (EC 2.3.1.48)	protein	15	0% helix, 7% strand	—

Interfaces

1 interface between chains.

A–B · 577 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

6F0Y · Rtt109 peptide bound to Asf1 · the same entry in another collection · chain A against A, TM-score 1.00
P32447 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1 (P32447) · a predicted model of the same protein · chain A against A, TM-score 0.87

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P32447
Elsewhere: RCSB PDB 6F0Y · PDBe 6F0Y · UniProt P32447

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