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Crystal structure of ADCP1 tandem agenet domain 3-4 in complex with H3K9ME2

Analyse Crystal structure of ADCP1 tandem agenet domain 3-4 in complex with H3K9ME2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IE6
Type: protein
Length: 160 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Agenet domain-containing protein; H3K9ME2
UniProt: Q500V5
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Agenet domain-containing protein	protein	150	9% helix, 49% strand	Q500V5
P	H3K9ME2	protein	10	40% helix, 20% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	330	0.63	0.79	32	empty

Interfaces

1 interface between chains.

A–P · 713 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

6IE6 · Crystal structure of ADCP1 tandem Agenet domain 3-4 in complex with H3K9me2 · the same entry in another collection · chain A against A, TM-score 1.00
Q500V5 · AlphaFold monomer V2.0 prediction for protein agenet domain (agd)-containing P1 (Q500V5) · 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 Q500V5
Elsewhere: RCSB PDB 6IE6 · PDBe 6IE6 · UniProt Q500V5

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