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Crystal structure of the SGF29 in complex with H3K4ME3

Analyse Crystal structure of the SGF29 in complex with H3K4ME3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MEA
Type: protein
Length: 166 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Saga-associated factor 29 homolog; Histone H3
UniProt: Q96ES7, Q92133
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Saga-associated factor 29 homolog	protein	162	6% helix, 40% strand	Q96ES7
B	Histone H3	protein	4	0% helix, 0% strand	Q92133

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	101	0.43	0.78	22	empty
2	58	0.32	0.76	13	empty

Interfaces

1 interface between chains.

A–B · 395 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

3MEA · Crystal structure of the SGF29 in complex with H3K4me3 · the same entry in another collection · chain A against A, TM-score 1.00
Q96ES7 · AlphaFold monomer V2.0 prediction for saga-associated factor 29 (Q96ES7) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q96ES7
Every structure of UniProt Q92133
Elsewhere: RCSB PDB 3MEA · PDBe 3MEA · UniProt Q96ES7 · UniProt Q92133

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