Structure of PDB 4ht3 Chain B

Receptor sequence

>4ht3B (length=393) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium)

TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKN
YAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRM
GKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRL
MGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIV
REFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVG
LIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSIS
AGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALES
SHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKAR

3D structure

• PDB: 4ht3 Allostery and substrate channeling in the tryptophan synthase bienzyme complex: evidence for two subunit conformations and four quaternary states.
• Chain: B
• Resolution: 1.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K87 E109 S377
• Catalytic site (residue number reindexed from 1): K86 E108 S376
• 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	B	H86 K87 T190 G232 G234 S235 N236 E350 S377 G378	H85 K86 T189 G231 G233 S234 N235 E349 S376 G377

Gene Ontology

Molecular Function

• GO:0004834 tryptophan synthase activity
• GO:0005515 protein binding
• GO:0016829 lyase activity
• GO:0042802 identical protein binding

Biological Process

• GO:0000162 tryptophan biosynthetic process
• GO:0006568 tryptophan metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:4ht3, PDBe:4ht3, PDBj:4ht3
• PDBsum: 4ht3
• PubMed: 23952479
• UniProt: P0A2K1|TRPB_SALTY Tryptophan synthase beta chain (Gene Name=trpB)