Structure of PDB 2j9y Chain B

Receptor sequence

>2j9yB (length=393)

TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKN
YAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRM
GKSEIIAETGAGNHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRL
MGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIV
REFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVG
LIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSIS
AGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALES
SHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKAR

3D structure

• PDB: 2j9y Betaq114N and Betat110V Mutations Reveal a Critically Important Role of the Substrate Alpha-Carboxylate Site in the Reaction Specificity of Tryptophan Synthase.
• Chain: B
• Resolution: 1.8 Å

Enzymatic activity

• 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	FOO	B	H86 K87 T110 G111 A112 G113 N114 H115 T190 G232 G233 G234 S235 N236 G303 E350 S377 G378 K392 A393 R394	H85 K86 T109 G110 A111 G112 N113 H114 T189 G231 G232 G233 S234 N235 G302 E349 S376 G377 K391 A392 R393
BS02	NA	B	G232 P270 F306 S308 V309	G231 P269 F305 S307 V308

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:2j9y, PDBe:2j9y, PDBj:2j9y
• PDBsum: 2j9y
• PubMed: 18004874
• UniProt: P0A2K1|TRPB_SALTY Tryptophan synthase beta chain (Gene Name=trpB)