Structure of PDB 4a2s Chain A

Receptor sequence
>4a2sA (length=247) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
PRYLKGWLEDVVQLSLRRPSVRASRQRPIISLNERILEFNKRNITAIIAY
YSRKSPSGLDVERDPIEYAKFMERYAVGLSIKTEEKYFNGSYETLRKIAS
SVSIPILMSDFIVKESQIDDAYNLGADTVLLIVKILTERELESLLEYARS
YGMEPLILINDENDLDIALRIGARFIGIFSMNFETGEINKENQRKLISMI
PSNVVKVAKLGISERNEIEELRKLGVNAFLISSSLMRNPEKIKELIE
3D structure
PDB4a2s Evolution of a designed retro-aldolase leads to complete active site remodeling.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y51 S53 S110 L159 F180 K210 L211
Catalytic site (residue number reindexed from 1) Y50 S52 S109 L158 F179 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 Y51 K83 K135 L159 N161 F180 F184 Y50 K82 K134 L158 N160 F179 F183
BS02 3NK A W8 P57 S58 M182 F184 K210 W7 P56 S57 M181 F183 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:4a2s, PDBe:4a2s, PDBj:4a2s
PDBsum4a2s
PubMed23748672
UniProtQ06121|TRPC_SACS2 Indole-3-glycerol phosphate synthase (Gene Name=trpC)

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