Research workbench

Crystal structure of OS79 from O. sativa in complex with udp.

Analyse Crystal structure of OS79 from O. sativa 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: 5TMB
Type: protein
Length: 451 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosyltransferase, OS79
EC: 2.4.1.-
UniProt: Q7XT97
Ligands: UDP
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycosyltransferase, OS79 (EC 2.4.1.-)	protein	451	45% helix, 13% strand	Q7XT97

Ligands and binding sites

UDP · Uridine-5'-diphosphate · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	698	0.80	0.84	70	UDP
2	62	0.38	0.79	15	empty
3	90	0.36	0.75	21	empty

Compared structures

5TMB · Crystal structure of Os79 from O. sativa in complex with UDP. · the same entry in another collection · chain A against A, TM-score 1.00
Q7XT97 · AlphaFold monomer V2.0 prediction for udp-glycosyltransferase 79 (Q7XT97) · a predicted model of the same protein · 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 Q7XT97
Elsewhere: RCSB PDB 5TMB · PDBe 5TMB · UniProt Q7XT97

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