MolNFT v1 · #49739 · protein

Structure of eugenol synthase from ocimum basilicum

2QX7 · Eugenol synthase 1: “Structure of eugenol synthase from ocimum basilicum”. X-ray diffraction, 1 ligand (NAP), 3 pockets (best druggability 0.86). MolNFT v1 #49739 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2QX7
Type: protein
Length: 620 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Eugenol synthase 1
UniProt: Q15GI4
Ligands: NAP
Pockets: 3 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Eugenol synthase 1	protein	310	43% helix, 16% strand	Q15GI4

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B

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	1085	0.86	0.86	114	NAP
2	126	0.44	0.77	23	empty
3	84	0.36	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 703 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2QX7 · Structure of Eugenol Synthase from Ocimum basilicum · the same entry in another collection · chain A against A, TM-score 1.00
Q15GI4 · AlphaFold monomer V2.0 prediction for eugenol synthase 1 (Q15GI4) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q15GI4
Elsewhere: RCSB PDB 2QX7 · PDBe 2QX7 · UniProt Q15GI4

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