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Crystal structure of teas C440W

Analyse Crystal structure of teas C440W in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HXC
Type: protein
Length: 516 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: FHP
Pockets: 6 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	5-epi-aristolochene synthase (EC 4.1.99.7)	protein	516	73% helix, 0% strand	Q40577

Ligands and binding sites

FHP · 1-hydroxy-3,7,11-trimethyldodeca-2,6,10-triene phosphonic acid · ligand · chains A

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	477	0.80	0.87	39	empty
2	566	0.75	0.82	57	FHP
3	239	0.56	0.78	25	empty
4	196	0.49	0.76	26	empty
5	71	0.46	0.83	17	empty

Compared structures

1HXC · Crystal structure of teas 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 1HXC · PDBe 1HXC · UniProt Q40577

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