Structure of PDB 1lbf Chain A

Receptor sequence
>1lbfA (length=247) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
PRYLKGWLKDVVQLSLRRPSFRASRQRPIISLNERILEFNKRNITAIIAE
YKRKSPSGLDVERDPIEYSKFMERYAVGLSILTEEKYFNGSYETLRKIAS
SVSIPILMKDFIVKESQIDDAYNLGADTVLLIVKILTERELESLLEYARS
YGMEPLIEINDENDLDIALRIGARFIGINSRDLETLEINKENQRKLISMI
PSNVVKVAESGISERNEIEELRKLGVNAFLIGSSLMRNPEKIKEFIL
3D structure
PDB1lbf The catalytic mechanism of indole-3-glycerol phosphate synthase: crystal structures of complexes of the enzyme from Sulfolobus solfataricus with substrate analogue, substrate, and product.
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 F89 K110 R182 L184 L187 S211 G212 L231 G233 S234 W7 E50 K52 S55 P56 S57 F88 K109 R181 L183 L186 S210 G211 L230 G232 S233 MOAD: Kd=0.014uM
PDBbind-CN: -logKd/Ki=7.85,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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1lbf, PDBe:1lbf, PDBj:1lbf
PDBsum1lbf
PubMed12054868
UniProtQ06121|TRPC_SACS2 Indole-3-glycerol phosphate synthase (Gene Name=trpC)

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