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Crystal structure of DAD2 N242I mutant

Analyse Crystal structure of DAD2 N242I mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UH8
Type: protein
Length: 528 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Decreased apical dominance 2
UniProt: L7MTK5
Ligands: MG, SO4
Pockets: 4 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Decreased apical dominance 2	protein	264	47% helix, 19% strand	L7MTK5

Ligands and binding sites

MG · Magnesium ion · metal · 7 copies · chains A, B
SO4 · Sulfate ion · ion · 3 copies · chains B
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	144	0.71	0.90	33	MES
2	130	0.66	0.87	29	MES
3	339	0.55	0.75	65	GOL, MG, SO4
4	204	0.46	0.74	26	empty

Interfaces

1 interface between chains.

A–B · 620 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6UH8 · Crystal structure of DAD2 N242I mutant · the same entry in another collection · chain A against A, TM-score 1.00

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 L7MTK5
Elsewhere: RCSB PDB 6UH8 · PDBe 6UH8 · UniProt L7MTK5

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