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Solution NMR structures of AF9 yeats domain in complex with histone H3 crotonylation at K18

Analyse Solution NMR structures of AF9 yeats domain in complex with histone H3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NDG
Type: protein
Length: 154 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein af-9; Histone H3 peptide
UniProt: P42568
Pockets: 1 · best druggability 0.26

Structure

solution nmr · 2 distinct chains · 8% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein af-9	protein	141	9% helix, 50% strand	P42568
B	Histone H3 peptide	protein	13	0% helix, 15% strand	—

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.26	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 559 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

2NDG · Solution NMR structures of AF9 yeats domain in complex with histone H3 crotonylation at… · 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 0.92

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
Elsewhere: RCSB PDB 2NDG · PDBe 2NDG · UniProt P42568

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