Research workbench

The structure of the inactive mutant G153R of lptc from E.COLI

Analyse The structure of the inactive mutant G153R of lptc from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4B54
Type: protein
Length: 250 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipopolysaccharide export system protein lptc
UniProt: I2Z3T4
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 70% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipopolysaccharide export system protein lptc	protein	125	0% helix, 69% strand	I2Z3T4
B	Lipopolysaccharide export system protein lptc	protein	125	0% helix, 71% strand	I2Z3T4

Ligands and binding sites

ACT · Acetate ion · 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	302	0.70	0.84	28	empty
2	64	0.30	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 744 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

4B54 · The Structure of the inactive mutant G153R of LptC from E. coli · 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 I2Z3T4
Elsewhere: RCSB PDB 4B54 · PDBe 4B54 · UniProt I2Z3T4

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