MolNFT v1 · #9466 · protein

Crystal structure of teas W273S/C440W

1HXG · 5-epi-aristolochene synthase: “Crystal structure of teas W273S/C440W”. X-ray diffraction, 1 ligand (MG), 7 pockets (best druggability 0.81). MolNFT v1 #9466 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1HXG
Type: protein
Length: 534 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 5-epi-aristolochene synthase
EC: 4.1.99.7
UniProt: Q40577
Ligands: MG
Pockets: 7 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	5-epi-aristolochene synthase (EC 4.1.99.7)	protein	534	71% helix, 0% strand	Q40577

Ligands and binding sites

MG · Magnesium ion · metal · chains A

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

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	517	0.81	0.88	51	empty
2	569	0.79	0.85	61	MG
3	254	0.59	0.79	25	empty
4	255	0.53	0.76	28	empty
5	79	0.52	0.85	17	empty

Compared structures

1HXG · Crystal structure of teas W273S/C440W · the same entry in another collection · chain A against A, TM-score 1.00
Q40577 · AlphaFold monomer V2.0 prediction for 5-epi-aristolochene synthase (Q40577) · 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 Q40577
Elsewhere: RCSB PDB 1HXG · PDBe 1HXG · UniProt Q40577

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