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Alpha-glucosyltransferase (agt) in complex with udp

Analyse Alpha-glucosyltransferase (agt) in complex with udp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XV5
Type: protein
Length: 401 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA alpha-glucosyltransferase
EC: 2.4.1.26
UniProt: P04519
Ligands: UDP, CL
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA alpha-glucosyltransferase (EC 2.4.1.26)	protein	401	42% helix, 19% strand	P04519

Ligands and binding sites

UDP · Uridine-5'-diphosphate · ligand · chains A
CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · 3 copies · chains A
GOL · Glycerol · additive · 2 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	491	0.79	0.86	61	CL, UDP, EDO, GOL
2	131	0.46	0.77	20	empty

Modifications

Observed in the structure: 2 modified (artifact).

Compared structures

1XV5 · alpha-glucosyltransferase (AGT) in complex with UDP · 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 P04519
Elsewhere: RCSB PDB 1XV5 · PDBe 1XV5 · UniProt P04519

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