MolNFT v1 · #45789 · protein

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

2NDG · Protein af-9: “Solution NMR structures of AF9 yeats domain in complex with histone H3 crotonylation at K18”. Solution nmr, 1 pocket (best druggability 0.26). MolNFT v1 #45789 on GenesisL1: 3D structure, binding sites and pockets in…

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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