Structure of PDB 4qys Chain A

Receptor sequence
>4qysA (length=408) Species: 273057 (Saccharolobus solfataricus P2) [Search protein sequence]
RIRIDLPQDEIPAQWYNILPDLPEELPPPQDPTGKSLELLKEVLPSKVLE
LEFAKERYVKIPDEVLERYLQVGRPTPIIRAKRLEEYLGNNIKIYLKMES
YTYTGSHKINSALAHVYYAKLDNAKFVTTETGAGQWGSSVALASALFRMK
AHIFMVRTSYYAKPYRKYMMQMYGAEVHPSPSDLLGIAISDAVEYAHKNG
GKYVVGSVVNSDIMFKTIAGMEAKKQMELIGEDPDYIIGVVGGGSNYAAL
AYPFLGDELRSGKVRRKYIASGSSEVPKMTKGVYKYDYPDTAKLLPMLKM
YTIGSDFVPPPVYAGGLRYHGVAPTLSLLISKGIVQARDYSQEESFKWAK
LFSELEGYIPAPETSHALPILAEIAEEAKKSGERKTVLVSFSGHGLLDLG
NYASVLFK
3D structure
PDB4qys TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases
ChainA
Resolution1.939 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K111 E133 S412
Catalytic site (residue number reindexed from 1) K108 E130 S392
Enzyme Commision number 4.2.1.20: tryptophan 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 PLP A H110 K111 G262 G263 G264 S265 N266 E383 S412 H107 K108 G242 G243 G244 S245 N246 E363 S392
BS02 SEP A K111 G135 A136 Q138 W139 G336 R338 E383 K108 G132 A133 Q135 W136 G316 R318 E363
Gene Ontology
Molecular Function
GO:0004834 tryptophan synthase activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0052684 L-serine hydro-lyase (adding indole, L-tryptophan-forming) activity
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0006568 tryptophan metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4qys, PDBe:4qys, PDBj:4qys
PDBsum4qys
PubMed25184516
UniProtQ97TX6|TRPB2_SACS2 Tryptophan synthase beta chain 2 (Gene Name=trpB2)

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