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Crystallization of HDAAM1 C-terminal fragment

Analyse Crystallization of HDAAM1 C-terminal fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J1D
Type: protein
Length: 395 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Disheveled-associated activator of morphogenesis 1
UniProt: Q9Y4D1
Ligands: PO4
Pockets: 4 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 70% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
G	Disheveled-associated activator of morphogenesis 1	protein	395	70% helix, 2% strand	Q9Y4D1

Ligands and binding sites

PO4 · Phosphate ion · ion · chains G
GOL · Glycerol · additive · chains G

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 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	160	0.43	0.74	25	empty
2	99	0.41	0.77	18	empty
3	50	0.29	0.75	16	empty
4	51	0.28	0.74	11	GOL

Compared structures

2J1D · Crystallization of hDaam1 C-terminal Fragment · the same entry in another collection · chain G against G, TM-score 1.00
Q9Y4D1 · AlphaFold monomer V2.0 prediction for disheveled-associated activator of morphogenesis 1… · a predicted model of the same protein · chain G against A, TM-score 0.98

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 Q9Y4D1
Elsewhere: RCSB PDB 2J1D · PDBe 2J1D · UniProt Q9Y4D1

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