Structure of PDB 4ou1 Chain A

Receptor sequence
>4ou1A (length=247) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
PRYLKGWLEDVVQLSLRRPSVRASRQRPIISLNERILEFNKRNITAIIAE
YKRKDPSGLDVERDPIEYAKFMERYAVGLFISTEEKYFNGSYETLRKIAS
SVSIPILMYDFIVKESQIDDAYNLGADTVALIVKILTERELESLLEYARS
YGMEPLIIINDENDLDIALRIGARFIGIAARDWETGEINKENQRKLISMI
PSNVVKVAKEGISERNEIEELRKLGVNAFLIGSSLMRNPEKIKELIE
3D structure
PDB4ou1 Small molecule probes to quantify the functional fraction of a specific protein in a cell with minimal folding equilibrium shifts.
ChainA
Resolution1.25 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 Y110 I159 A180 K210 E211
Catalytic site (residue number reindexed from 1) E50 K52 Y109 I158 A179 K209 E210
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 2V7 A D56 P57 F89 Y110 R182 D183 W184 G187 K210 E211 D55 P56 F88 Y109 R181 D182 W183 G186 K209 E210
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4ou1, PDBe:4ou1, PDBj:4ou1
PDBsum4ou1
PubMed24591605
UniProtQ06121|TRPC_SACS2 Indole-3-glycerol phosphate synthase (Gene Name=trpC)

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