Research workbench

Structural evidence for ammonia tunelling across the (beta- ALPHA)8-barrel of the imidazole glycerol phosphate synthase bienzyme complex

Analyse Structural evidence for ammonia tunelling across the (beta- ALPHA)8-barrel of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1K9V
Type: protein
Length: 200 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amidotransferase hish
EC: 2.4.2.-
UniProt: Q9X0C8
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
F	Amidotransferase hish (EC 2.4.2.-)	protein	200	28% helix, 36% strand	Q9X0C8

Ligands and binding sites

ACY · Acetic acid · additive · chains F

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	54	0.37	0.80	15	ACY

Compared structures

1K9V · Structural evidence for ammonia tunelling across the (beta-alpha)8-barrel of the… · the same entry in another collection · chain F against F, TM-score 1.00
Q9X0C8 · AlphaFold monomer V2.0 prediction for imidazole glycerol phosphate synthase subunit hish… · a predicted model of the same protein · chain F against A, TM-score 0.99

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 Q9X0C8
Elsewhere: RCSB PDB 1K9V · PDBe 1K9V · UniProt Q9X0C8

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