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Crystal structure of a cyclase subunit of imidazolglycerolphosphate synthase

Analyse Crystal structure of a cyclase subunit of imidazolglycerolphosphate synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VH7
Type: protein
Length: 250 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Imidazole glycerol phosphate synthase subunit hisf
EC: 4.1.3.-
UniProt: Q9X0C6
Ligands: PO4
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Imidazole glycerol phosphate synthase subunit hisf (EC 4.1.3.-)	protein	250	40% helix, 25% strand	Q9X0C6

Ligands and binding sites

PO4 · Phosphate ion · ion · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	344	0.61	0.78	38	PO4

Compared structures

1VH7 · Crystal structure of a cyclase subunit of imidazolglycerolphosphate synthase · the same entry in another collection · chain A against A, TM-score 1.00
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
Elsewhere: RCSB PDB 1VH7 · PDBe 1VH7 · UniProt Q9X0C6

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