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A rice glycosyltransferase in complex with udp and rex

Analyse A rice glycosyltransferase in complex with udp and rex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ES0
Type: protein
Length: 407 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosyltransferase
EC: 2.4.1.-
UniProt: Q0DPB7
Ligands: 3E6, UDP
Pockets: 1 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycosyltransferase (EC 2.4.1.-)	protein	407	44% helix, 15% strand	Q0DPB7

Ligands and binding sites

3E6 · Rebaudioside A2 · ligand · chains A
UDP · Uridine-5'-diphosphate · ligand · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A
MPO · 3[N-morpholino]propane sulfonic acid · additive · chains A
GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	767	0.80	0.83	80	3E6, UDP, EDO

Compared structures

7ES0 · a rice glycosyltransferase in complex with UDP and REX · 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 Q0DPB7
Elsewhere: RCSB PDB 7ES0 · PDBe 7ES0 · UniProt Q0DPB7

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