Structure of PDB 4a29 Chain A

Receptor sequence
>4a29A (length=247) Species: 32630 (synthetic construct) [Search protein sequence]
PRYLKGWLEDVVQLSLRRPSVRASRQRPIISLNERILEFNKRNITAIIAV
YERKSPSGLDVERDPIEYAKFMERYAVGLSITTEEKYFNGSYETLRKIAS
SVSIPILMSDFIVKESQIDDAYNLGADTVLLIVKILTERELESLLEYARS
YGMEPLILINDENDLDIALRIGARFIGIMSRDFETGEINKENQRKLISMI
PSNVVKVAKLGISERNEIEELRKLGVNAFLISSSLMRNPEKIKELIE
3D structure
PDB4a29 Evolution of a designed retro-aldolase leads to complete active site remodeling.
ChainA
Resolution1.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V51 E53 S110 L159 M180 K210 L211
Catalytic site (residue number reindexed from 1) V50 E52 S109 L158 M179 K209 L210
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 3NK A M180 R182 G187 K210 M179 R181 G186 K209
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:4a29, PDBe:4a29, PDBj:4a29
PDBsum4a29
PubMed23748672
UniProtQ06121|TRPC_SACS2 Indole-3-glycerol phosphate synthase (Gene Name=trpC)

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