Structure of PDB 5tcj Chain F

Receptor sequence
>5tcjF (length=399) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
TSHDPDSGGHFGGPSGWGGRYVPEALMAVIEEVTAAYQKERVSQDFLDDL
DRLQANYAGRPSPLYEATRLSQHAGSARIFLKREDLNHTGSHKINNVLGQ
ALLARRMGKTRVIAETGAGQHGVATATACALLGLDCVIYMGGIDTARQAL
NVARMRLLGAEVVAVQTGSKTLKDAINEAFRDWVANADNTYYCFGTAAGP
HPFPTMVRDFQRIIGMEARVQIQGQAGRLPDAVVACVGGGSNAIGIFHAF
LDDPGVRLVGFEAAGDGVETGRHAATFTAGSPGAFHGSFSYLLQDEDGQT
IESHSISAGLDYPGVGPEHAWLKEAGRVDYRPITDSEAMDAFGLLCRMEG
IIPAIESAHAVAGALKLGVELGRGAVIVVNLSGRGDKDVETAAKWFGLL
3D structure
PDB5tcj A small-molecule allosteric inhibitor of Mycobacterium tuberculosis tryptophan synthase.
ChainF
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K101 E123 S390
Catalytic site (residue number reindexed from 1) K93 E115 S382
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 P1T F H100 K101 T124 G125 A126 Q128 H129 T204 G246 G248 S249 N250 G317 E364 S390 G391 H92 K93 T116 G117 A118 Q120 H121 T196 G238 G240 S241 N242 G309 E356 S382 G383
BS02 79V F I184 F188 Y200 F202 P208 H294 I176 F180 Y192 F194 P200 H286
Gene Ontology
Molecular Function
GO:0004834 tryptophan synthase activity
GO:0016829 lyase activity
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0006568 tryptophan metabolic process
GO:1901605 alpha-amino acid 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:5tcj, PDBe:5tcj, PDBj:5tcj
PDBsum5tcj
PubMed28671682
UniProtP9WFX9|TRPB_MYCTU Tryptophan synthase beta chain (Gene Name=trpB)

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