Structure of PDB 4qys Chain B

Receptor sequence
>4qysB (length=418) Species: 273057 (Saccharolobus solfataricus P2) [Search protein sequence]
RIRIDLPQDEIPAQWYNILPDLPEELPPPQELLKEVLPSKVLELEFAKER
YVKIPDEVLERYLQVGRPTPIIRAKRLEEYLGNNIKIYLKMESYTYTGSH
KINSALAHVYYAKLDNAKFVTTETGAGQWGSSVALASALFRMKAHIFMVR
TSYYAKPYRKYMMQMYGAEVHPSPSDLTEFGRQLLAKDSNHPGSLGIAIS
DAVEYAHKNGGKYVVGSVVNSDIMFKTIAGMEAKKQMELIGEDPDYIIGV
VGGGSNYAALAYPFLGDELRSGKVRRKYIASGSSEVPKMTKGVYKYDYPD
TAKLLPMLKMYTIGSDFVPPPVYAGGLRYHGVAPTLSLLISKGIVQARDY
SQEESFKWAKLFSELEGYIPAPETSHALPILAEIAEEAKKSGERKTVLVS
FSGHGLLDLGNYASVLFK
3D structure
PDB4qys TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases
ChainB
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) K101 E123 S402
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 PLR B H110 K111 G262 G263 G264 S265 N266 E383 S412 H100 K101 G252 G253 G254 S255 N256 E373 S402
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
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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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