Research workbench

AF9 yeats in complex with histone H3 crotonylation at K9

Analyse AF9 yeats in complex with histone H3 crotonylation at K9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HJB
Type: protein
Length: 148 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein af-9; Peptide of histone H3.1
UniProt: P42568, P68431

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein af-9	protein	140	8% helix, 51% strand	P42568
B	Peptide of histone H3.1	protein	8	0% helix, 25% strand	P68431

Interfaces

1 interface between chains.

A–B · 623 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

5HJB · AF9 YEATS in complex with histone H3 Crotonylation at K9 · the same entry in another collection · chain A against A, TM-score 1.00
P42568 · AlphaFold monomer V2.0 prediction for protein af-9 (P42568) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P42568
Every structure of UniProt P68431
Elsewhere: RCSB PDB 5HJB · PDBe 5HJB · UniProt P42568 · UniProt P68431

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