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Pentalenene synthase

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

PDB: 1PS1
Type: protein
Length: 608 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pentalenene synthase
EC: 4.6.1.5
UniProt: Q55012
Ligands: PBM
Pockets: 3 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pentalenene synthase (EC 4.6.1.5)	protein	304	72% helix, 0% strand	Q55012

Ligands and binding sites

PBM · Trimethyl lead ion · metal · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1192	0.82	0.83	88	empty
2	752	0.75	0.80	57	empty
3	759	0.74	0.79	59	empty

Interfaces

1 interface between chains.

A–B · 962 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1PS1 · Pentalenene synthase · the same entry in another collection · chain A against A, TM-score 1.00
Q55012 · AlphaFold monomer V2.0 prediction for pentalenene synthase (Q55012) · a predicted model of the same protein · chain A 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 Q55012
Elsewhere: RCSB PDB 1PS1 · PDBe 1PS1 · UniProt Q55012

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