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Crystal structure of human glycogenin-1 (GYG1), apo form

Analyse Crystal structure of human glycogenin-1 (GYG1), apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3Q4S
Type: protein
Length: 251 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycogenin-1
EC: 2.4.1.186
UniProt: P46976
Ligands: CL
Pockets: 2 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycogenin-1 (EC 2.4.1.186)	protein	251	43% helix, 20% strand	P46976

Ligands and binding sites

CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · 9 copies · chains A

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

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	164	0.47	0.76	24	EDO
2	98	0.37	0.75	19	empty

Compared structures

3Q4S · Crystal Structure of Human Glycogenin-1 (GYG1), apo form · the same entry in another collection · chain A against A, TM-score 1.00
P46976 · AlphaFold monomer V2.0 prediction for glycogenin-1 (P46976) · 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 P46976
Elsewhere: RCSB PDB 3Q4S · PDBe 3Q4S · UniProt P46976

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