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The apo form of idole-3-glycerol phosphate synthase (trpc) form mycobacterium tuberculosis

Analyse The apo form of idole-3-glycerol phosphate synthase (trpc) form mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FB7
Type: protein
Length: 266 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Indole-3-glycerol phosphate synthase
EC: 4.1.1.48
UniProt: P0A632
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Indole-3-glycerol phosphate synthase (EC 4.1.1.48)	protein	266	45% helix, 15% strand	P0A632

Ligands and binding sites

BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · 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	136	0.71	0.91	27	empty
2	53	0.25	0.73	19	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

4FB7 · The apo form of idole-3-glycerol phosphate synthase (TrpC) form Mycobacterium tuberculosis · 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 P0A632
Elsewhere: RCSB PDB 4FB7 · PDBe 4FB7 · UniProt P0A632

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