Structure of PDB 7jmq Chain B

Receptor sequence

>7jmqB (length=396) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2)

TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKN
YAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRM
GKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRL
MGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIV
REFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVG
LIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSIS
AGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALES
SHALAHALKMMREQPEKEQLLVVNLAGRGDKDIFTVHDILKARGEI

3D structure

• PDB: 7jmq The external aldimine form of mutant beta-S377A Salmonella thypi tryptophan synthase in open conformation showing dual side chain conformations for the residue beta-Q114, sodium ion at the metal coordination site, and F9 inhibitor at the alpha-site. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring.
• Chain: B
• Resolution: 1.6 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	KOU	B	H86 K87 T110 G111 A112 Q114 H115 T190 G232 G234 S235 N236 G303 D305 E350	H85 K86 T109 G110 A111 Q113 H114 T189 G231 G233 S234 N235 G302 D304 E349

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:7jmq, PDBe:7jmq, PDBj:7jmq
• PDBsum: 7jmq
• UniProt: P0A2K1|TRPB_SALTY Tryptophan synthase beta chain (Gene Name=trpB)