MolNFT v1 · #9129 · protein

N219L pentalenene synthase

1HM4: “N219L pentalenene synthase”. X-ray diffraction, 5 pockets (best druggability 0.82). MolNFT v1 #9129 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1HM4
Type: protein
Length: 589 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
Pockets: 5 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 69% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pentalenene synthase (EC 4.6.1.5)	protein	289	70% helix, 0% strand	Q55012
B	Pentalenene synthase (EC 4.6.1.5)	protein	300	69% helix, 0% strand	Q55012

Pockets

5 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	1149	0.82	0.83	89	empty
2	661	0.76	0.82	50	empty
3	684	0.76	0.81	58	empty
4	52	0.29	0.75	14	empty
5	52	0.29	0.75	12	empty

Interfaces

1 interface between chains.

A–B · 1009 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1HM4 · N219L 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 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 Q55012
Elsewhere: RCSB PDB 1HM4 · PDBe 1HM4 · UniProt Q55012

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.