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Crystal structure of UDP-SrUGT76G1

Analyse Crystal structure of UDP-SrUGT76G1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KVI
Type: protein
Length: 433 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.598
Source: Stevia rebaudiana
Molecule: UDP-glycosyltransferase 76G1
EC: 2.4.1.-
UniProt: Q6VAB4
Ligands: UDP
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · resolution 2.598 · 1 distinct chain · 42% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	UDP-glycosyltransferase 76G1 (EC 2.4.1.-)	protein	433	42% helix, 15% strand	Q6VAB4

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	904	0.81	0.83	76	UDP
2	69	0.39	0.79	12	empty
3	71	0.34	0.75	12	empty

Compared structures

6KVI · Crystal structure of udp-SRUGT76G1 · the same entry in another collection · chain A against A, TM-score 1.00
Q6VAB4 · AlphaFold monomer V2.0 prediction for udp-glycosyltransferase 76G1 (Q6VAB4) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q6VAB4
Elsewhere: RCSB PDB 6KVI · PDBe 6KVI · UniProt Q6VAB4

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