MolNFT v1 · #163145 · protein

Light-regulation of imidazole glycerol phosphate synthase by interference with its allosteric machinery through photo-sensitive unnatural amino acids

6RU0: “Light-regulation of imidazole glycerol phosphate synthase by interference with its allosteric machinery…”. X-ray diffraction, 1 ligand (PO4). MolNFT v1 #163145 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6RU0
Type: protein
Length: 1,358 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9X0C6, Q9X0C8
Ligands: PO4

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E	—	protein	253	—	Q9X0C6
B, D	—	protein	200	—	Q9X0C8
F	—	protein	199	—	Q9X0C8

Ligands and binding sites

PO4 · Phosphate ion · ion · 3 copies · chains A, C, E

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6RU0 · Light-Regulation of Imidazole Glycerol Phosphate Synthase by Interference with its… · 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
Q9X0C6 · AlphaFold monomer V2.0 prediction for imidazole glycerol phosphate synthase subunit hisf… · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q9X0C6
Every structure of UniProt Q9X0C8
Elsewhere: RCSB PDB 6RU0 · PDBe 6RU0 · UniProt Q9X0C6 · UniProt Q9X0C8

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