MolNFT v1 · #122386 · protein

Crystal structure of prenyltransferase prib ternary complex with L- tryptophan and dimethylallyl thiolodiphosphate (dmspp)

5INJ: “Crystal structure of prenyltransferase prib ternary complex with L- tryptophan and dimethylallyl…”. X-ray diffraction, 2 ligands (TRP, DST), 2 pockets (best druggability 0.78). MolNFT v1 #122386 on GenesisL1: 3D structure, binding…

PDB: 5INJ
Type: protein
Length: 355 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prenyltransferase
Ligands: TRP, DST
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Prenyltransferase	protein	355	38% helix, 21% strand	—

Ligands and binding sites

TRP · Tryptophan · ligand · chains A
DST · Dimethylallyl S-thiolodiphosphate · ligand · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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	260	0.78	0.90	48	TRP, DST
2	134	0.49	0.79	26	empty

Compared structures

5INJ · Crystal Structure of Prenyltransferase PriB Ternary Complex with L-Tryptophan 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
Elsewhere: RCSB PDB 5INJ · PDBe 5INJ

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