Structure of PDB 1kfk Chain B

Receptor sequence

>1kfkB (length=392) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2)

TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKN
YAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRM
GKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRL
MGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIV
REFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVG
LIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSIS
AGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALES
SHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKA

3D structure

• PDB: 1kfk On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase.
• Chain: B
• Resolution: 2.4 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 C230 G232 G233 G234 S235 N236 E350 S377 G378	H85 K86 T189 C229 G231 G232 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:1kfk, PDBe:1kfk, PDBj:1kfk
• PDBsum: 1kfk
• PubMed: 12460570
• UniProt: P0A2K1|TRPB_SALTY Tryptophan synthase beta chain (Gene Name=trpB)