Research workbench

Pgld from campylobacter jejuni nctc 11168 in complex with 5-(2- furanyl)-1H-pyrazole-3-carboxylic acid

Analyse Pgld from campylobacter jejuni nctc 11168 in complex with 5-(2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TYH
Type: protein
Length: 185 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-N-acetylbacillosamine N-acetyltransferase
EC: 2.3.1.203
UniProt: Q0P9D1
Ligands: 7O4
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-N-acetylbacillosamine N-acetyltransferase (EC 2.3.1.203)	protein	185	15% helix, 26% strand	Q0P9D1

Ligands and binding sites

7O4 · 3-(furan-2-yl)-1H-pyrazole-5-carboxylic acid · ligand · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.40	0.82	16	empty

Compared structures

5TYH · PglD from Campylobacter jejuni NCTC 11168 in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
Q0P9D1 · AlphaFold monomer V2.0 prediction for udp-N-acetylbacillosamine N-acetyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q0P9D1
Elsewhere: RCSB PDB 5TYH · PDBe 5TYH · UniProt Q0P9D1

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