MolNFT v1 · #118553 · protein

E.COLI glpg Y205F mutant complexed with aldehyde inhibitor in DMPC/CHAPSO bicelle

5F5K · Rhomboid protease glpg: “E.COLI glpg Y205F mutant complexed with aldehyde inhibitor in DMPC/CHAPSO bicelle”. X-ray diffraction, 2 pockets (best druggability 0.41). MolNFT v1 #118553 on GenesisL1: 3D structure, binding sites and…

PDB: 5F5K
Type: protein
Length: 182 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rhomboid protease glpg; Peptidic derivative of gurken: ACE-arg-lys-val-arg-met-ala…
EC: 3.4.21.105
UniProt: A0A0J2E248
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 73% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rhomboid protease glpg (EC 3.4.21.105)	protein	178	75% helix, 2% strand	A0A0J2E248
B	Peptidic derivative of gurken: ACE-arg-lys-val-arg-met-ala- aldehyde	protein	4	0% helix, 50% strand	—

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.41	0.80	13	empty
2	75	0.34	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 488 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

5F5K · E.Coli GlpG Y205F mutant complexed with aldehyde inhibitor in DMPC/CHAPSO bicelle · 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 A0A0J2E248
Elsewhere: RCSB PDB 5F5K · PDBe 5F5K · UniProt A0A0J2E248

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