Structure of PDB 1lbl Chain A

Receptor sequence

>1lblA (length=247) Species: 2287 (Saccharolobus solfataricus)

PRYLKGWLKDVVQLSLRRPSFRASRQRPIISLNERILEFNKRNITAIIAE
YKRKSPSGLDVERDPIEYSKFMERYAVGLSILTEEKYFNGSYETLRKIAS
SVSIPILMKDFIVKESQIDDAYNLGADTVLLIVKILTERELESLLEYARS
YGMEPLIEINDENDLDIALRIGARFIGINSRDLETLEINKENQRKLISMI
PSNVVKVAESGISERNEIEELRKLGVNAFLIGSSLMRNPEKIKEFIL

3D structure

• PDB: 1lbl The catalytic mechanism of indole-3-glycerol phosphate synthase: Crystal structures of complexes of the enzyme from Sulfolobus solfataricus with the substrate analogue, substrate, and product
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E51 K53 K110 E159 N180 E210 S211
• Catalytic site (residue number reindexed from 1): E50 K52 K109 E158 N179 E209 S210
• Enzyme Commision number: 4.1.1.48: indole-3-glycerol-phosphate synthase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	137	A	W8 E51 K53 S56 P57 S58 K110 R182 L184 L187 E210 S211 L231 G233 S234	W7 E50 K52 S55 P56 S57 K109 R181 L183 L186 E209 S210 L230 G232 S233	MOAD: Kd=0.014uM

Gene Ontology

Molecular Function

• GO:0004425 indole-3-glycerol-phosphate synthase activity
• GO:0004640 phosphoribosylanthranilate isomerase activity
• GO:0016830 carbon-carbon lyase activity
• GO:0016831 carboxy-lyase activity

Biological Process

• GO:0000162 tryptophan biosynthetic process
• GO:0006568 tryptophan metabolic process

External links

• PDB: RCSB:1lbl, PDBe:1lbl, PDBj:1lbl
• PDBsum: 1lbl
• PubMed: 12054868
• UniProt: Q06121|TRPC_SACS2 Indole-3-glycerol phosphate synthase (Gene Name=trpC)