Structure of PDB 6y88 Chain E

Receptor sequence
>6y88E (length=265) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
SVPTVLQKILARKAEEVAERRARVNLAEVERLARSADAPRGFANALLERA
KRKEPAVIAEIKKASPSKGVLREHFVPAEIARSYEAGGAACLSVLTDVDF
FQGADAYLKEARAACALPVIRKDFMIDPYQIVEARAIGADCILLIVSALD
DVLMAELAATAKSVGLDVLVEVHDGTELERALKTLDTPLVGINNRNLHTF
EVSLETTLDLLPEIPRDRLVVTESGILNRADVELMEVSEVYAFLVGEAFM
RADDPGLELKRLFFQ
3D structure
PDB6y88 Structure and kinetics of indole-3-glycerol phosphate synthase from Pseudomonas aeruginosa : Decarboxylation is not essential for indole formation.
ChainE
Resolution2.09983 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E61 K63 K123 E172 N194 E224 S225
Catalytic site (residue number reindexed from 1) E60 K62 K122 E171 N193 E223 S224
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 E E61 K63 P67 S68 F102 K123 L198 E224 S225 L245 G247 E248 E60 K62 P66 S67 F101 K122 L197 E223 S224 L244 G246 E247
BS02 GOL E R73 H75 V77 E80 I81 R72 H74 V76 E79 I80
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:6y88, PDBe:6y88, PDBj:6y88
PDBsum6y88
PubMed32928960
UniProtP20577|TRPC_PSEAE Indole-3-glycerol phosphate synthase (Gene Name=trpC)

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