Structure of PDB 4hpx Chain B Binding Site BS03

Receptor Information
>4hpx Chain B (length=395) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKN
YAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRM
GKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRL
MGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIV
REFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVG
LIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSIS
AGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALES
SHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKARGE
Ligand information
Ligand IDBZI
InChIInChI=1S/C7H6N2/c1-2-4-7-6(3-1)8-5-9-7/h1-5H,(H,8,9)
InChIKeyHYZJCKYKOHLVJF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04n2c1ccccc1nc2
OpenEye OEToolkits 1.5.0c1ccc2c(c1)[nH]cn2
CACTVS 3.341[nH]1cnc2ccccc12
FormulaC7 H6 N2
NameBENZIMIDAZOLE
ChEMBLCHEMBL306226
DrugBankDB02962
ZINCZINC000000331902
PDB chain4hpx Chain B Residue 403 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4hpx Allostery and substrate channeling in the tryptophan synthase bienzyme complex: evidence for two subunit conformations and four quaternary states.
Resolution1.65 Å
Binding residue
(original residue number in PDB)		A136 K137
Binding residue
(residue number reindexed from 1)		A135 K136
Annotation score1
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.
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4hpx, PDBe:4hpx, PDBj:4hpx
PDBsum4hpx
PubMed23952479
UniProtP0A2K1|TRPB_SALTY Tryptophan synthase beta chain (Gene Name=trpB)

[Back to BioLiP]