Structure of PDB 6xnc Chain B

Receptor sequence
>6xncB (length=396) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium) [Search protein sequence]
TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKN
YAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRM
GKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRL
MGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIV
REFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVG
LIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSIS
AGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALES
SHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKARGEI
3D structure
PDB6xnc Structural Basis of the Stereochemistry of Inhibition of Tryptophan Synthase by Tryptophan and Derivatives.
ChainB
Resolution2.11 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 NA B G232 P270 F306 S308 G231 P269 F305 S307
BS02 PLP B H86 K87 Q114 T190 C230 G232 G233 G234 S235 N236 E350 S377 G378 H85 K86 Q113 T189 C229 G231 G232 G233 S234 N235 E349 S376 G377
BS03 TRP B K87 E109 T110 G111 A112 Q114 H115 T190 F306 K86 E108 T109 G110 A111 Q113 H114 T189 F305
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:6xnc, PDBe:6xnc, PDBj:6xnc
PDBsum6xnc
PubMed33428374
UniProtP0A2K1|TRPB_SALTY Tryptophan synthase beta chain (Gene Name=trpB)

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