Structure of PDB 4hpx Chain B

Receptor sequence

>4hpxB (length=395) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium)

TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKN
YAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRM
GKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRL
MGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIV
REFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVG
LIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSIS
AGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALES
SHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKARGE

3D structure

• PDB: 4hpx Allostery and substrate channeling in the tryptophan synthase bienzyme complex: evidence for two subunit conformations and four quaternary states.
• Chain: B
• Resolution: 1.65 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	BZI	B	K87 E109 L166 G189 T190 G232 G233 F306	K86 E108 L165 G188 T189 G231 G232 F305
BS02	BZI	B	T3 L5 N6	T2 L4 N5
BS03	BZI	B	A136 K137	A135 K136
BS04	0JO	B	H86 K87 T110 G111 A112 G113 Q114 H115 T190 G232 G233 G234 S235 N236 G303 E350 S377 G378	H85 K86 T109 G110 A111 G112 Q113 H114 T189 G231 G232 G233 S234 N235 G302 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:4hpx, PDBe:4hpx, PDBj:4hpx
• PDBsum: 4hpx
• PubMed: 23952479
• UniProt: P0A2K1|TRPB_SALTY Tryptophan synthase beta chain (Gene Name=trpB)