Research workbench

Simvastatin synthase (lovd), from aspergillus terreus, S5 mutant, S76A mutant, complex with simvastatin

Analyse Simvastatin synthase (lovd), from aspergillus terreus, S5 mutant, S76A mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HLF
Type: protein
Length: 425 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transesterase
UniProt: Q9Y7D1
Ligands: SIM
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transesterase	protein	425	33% helix, 17% strand	Q9Y7D1

Ligands and binding sites

SIM · Simvastatin acid · ligand · chains A

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

Pockets

2 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	259	0.60	0.79	28	SIM
2	51	0.27	0.74	12	empty

Compared structures

3HLF · Simvastatin Synthase (LovD), from Aspergillus terreus, S5 mutant, S76A mutant, complex… · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y7D1 · AlphaFold monomer V2.0 prediction for monacolin J acid methylbutanoyltransferase (Q9Y7D1) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9Y7D1
Elsewhere: RCSB PDB 3HLF · PDBe 3HLF · UniProt Q9Y7D1

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