Research workbench

Apo form of a mutant of glycogenin in which ASP159 is replaced by ser

Analyse Apo form of a mutant of glycogenin in which ASP159 is replaced by ser in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZCY
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycogenin-1
EC: 2.4.1.186
UniProt: P13280
Ligands: SO4
Pockets: 3 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycogenin-1 (EC 2.4.1.186)	protein	257	46% helix, 18% strand	P13280

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

Pockets

3 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	207	0.49	0.76	25	empty
2	115	0.46	0.78	18	empty
3	60	0.34	0.76	15	empty

Compared structures

1ZCY · apo form of a mutant of glycogenin in which Asp159 is replaced by Ser · the same entry in another collection · chain A against A, TM-score 1.00
P13280 · AlphaFold monomer V2.0 prediction for glycogenin-1 (P13280) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P13280
Elsewhere: RCSB PDB 1ZCY · PDBe 1ZCY · UniProt P13280

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