MolNFT v1 · #32827 · protein

Structure and activity of a flavonoid 3-O glucosyltransferase reveals the basis for plant natural product modification

2C1Z · Udp-glucose flavonoid 3-O glycosyltransferase: “Structure and activity of a flavonoid 3-O glucosyltransferase reveals the basis for plant natural product…”. X-ray diffraction, 2 ligands (KMP, U2F), 3 pockets (best druggability…

PDB: 2C1Z
Type: protein
Length: 439 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-glucose flavonoid 3-O glycosyltransferase
EC: 2.4.1.91
UniProt: O22304
Ligands: KMP, U2F
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-glucose flavonoid 3-O glycosyltransferase (EC 2.4.1.91)	protein	439	48% helix, 14% strand	O22304

Ligands and binding sites

KMP · 3,5,7-trihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one · ligand · chains A
U2F · Uridine-5'-diphosphate-2-deoxy-2-fluoro-alpha-D-glucose · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	773	0.76	0.80	78	KMP, U2F
2	76	0.57	0.87	18	empty
3	100	0.41	0.77	15	empty

Compared structures

2C1Z · Structure and activity of a flavonoid 3-O glucosyltransferase reveals the basis for plant… · 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 O22304
Elsewhere: RCSB PDB 2C1Z · PDBe 2C1Z · UniProt O22304

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