Structure of PDB 2j9z Chain B Binding Site BS02
Receptor Information
>2j9z Chain B (length=392) [
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TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKN
YAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRM
GKSEIIAEVGAGNHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRL
MGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIV
REFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVG
LIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSIS
AGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALES
SHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKA
Ligand information
Ligand ID
NA
InChI
InChI=1S/Na/q+1
InChIKey
FKNQFGJONOIPTF-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Na+]
Formula
Na
Name
SODIUM ION
ChEMBL
DrugBank
DB14516
ZINC
PDB chain
2j9z Chain B Residue 1396 [
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Receptor-Ligand Complex Structure
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PDB
2j9z
Betaq114N and Betat110V Mutations Reveal a Critically Important Role of the Substrate Alpha-Carboxylate Site in the Reaction Specificity of Tryptophan Synthase.
Resolution
1.8 Å
Binding residue
(original residue number in PDB)
G232 P270 F306 S308
Binding residue
(residue number reindexed from 1)
G231 P269 F305 S307
Annotation score
1
Enzymatic activity
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
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:2j9z
,
PDBe:2j9z
,
PDBj:2j9z
PDBsum
2j9z
PubMed
18004874
UniProt
P0A2K1
|TRPB_SALTY Tryptophan synthase beta chain (Gene Name=trpB)
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