Research workbench

Pylc in complex with L-lysine-ne-D-ornithine (cocrystallized with L- lysine and D-ornithine)

Analyse Pylc in complex with L-lysine-ne-D-ornithine (cocrystallized with L- lysine and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FFP
Type: protein
Length: 353 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein
UniProt: Q46E79
Ligands: ADP, 0TF, MG, PO4
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein	protein	353	30% helix, 32% strand	Q46E79

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A
0TF · N~6~-D-ornithyl-L-lysine · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
PO4 · Phosphate ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	524	0.79	0.86	65	0TF, ADP, PO4, MG

Compared structures

4FFP · PylC in complex with L-lysine-Ne-D-ornithine (cocrystallized with L-lysine and… · 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 Q46E79
Elsewhere: RCSB PDB 4FFP · PDBe 4FFP · UniProt Q46E79

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