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Crystal structure of mycobacterium tuberculosis indole glycerol phosphate synthase (igps) in complex with 5-fluoroanthranilate

Analyse Crystal structure of mycobacterium tuberculosis indole glycerol phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3T78
Type: protein
Length: 257 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
Ligands: 5RG
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Indole-3-glycerol phosphate synthase (EC 4.1.1.48)	protein	257	46% helix, 16% strand	P0A632

Ligands and binding sites

5RG · 2-amino-5-fluorobenzoic acid · ligand · chains A
ACT · Acetate ion · additive · 3 copies · chains A
MLI · Malonate ion · additive · 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	180	0.75	0.91	31	5RG, MLI, ACT

Compared structures

3T78 · Crystal Structure of Mycobacterium tuberculosis Indole Glycerol Phosphate Synthase (IGPS)… · 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 3T78 · PDBe 3T78 · UniProt P0A632

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