Research workbench

Pimaricin type I pks thioesterase domain (holo pim te)

Analyse Pimaricin type I pks thioesterase domain (holo pim te) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7VO5
Type: protein
Length: 276 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SCNS4
UniProt: F1CLA7
Ligands: 81E
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SCNS4	protein	276	40% helix, 14% strand	F1CLA7

Ligands and binding sites

81E · (1R,3S,5E,7S,11R,13E,15E,17E,19E,21R,23S,24R,25S)-11, 24-dimethyl-1,3,7,21,25-pentakis(oxidanyl)-10,27-dioxabicyclo[21.3.1]heptacosa-5,13,15,17,19-pentaen-9-one · ligand · chains A

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

Pockets

4 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	481	0.76	0.84	53	81E
2	118	0.44	0.77	18	empty
3	54	0.42	0.82	12	empty
4	51	0.34	0.79	19	empty

Compared structures

7VO5 · Pimaricin type I PKS thioesterase domain (holo Pim TE) · the same entry in another collection · 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 F1CLA7
Elsewhere: RCSB PDB 7VO5 · PDBe 7VO5 · UniProt F1CLA7

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