Structure of PDB 5bne Chain D

Receptor sequence
>5bneD (length=327) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
PSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKAP
TADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGNLSTMAAIVVAAAG
VPVVKHGNRAGADTLEALGVRIDLGPDLVARSLAEVGIGFCFAPRFHPSY
RHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAFADLAEVMAGVFAA
RRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLTFDPAGFGFARAQL
DDAQANAAAVRAVLGGARGPVRDAVVLNAAGAIVAHAGLSSAEWLPAWEE
GLRRASAAIDTGAAEQLLARWVRFGRQ
3D structure
PDB5bne Binding and mimicking of the phosphate-rich substrate, PRPP.
ChainD
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V106
Catalytic site (residue number reindexed from 1) V82
Enzyme Commision number 2.4.2.18: anthranilate phosphoribosyltransferase.
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 7P3 D M86 N138 A179 P180 H183 Y186 R187 A190 R193 R194 M62 N108 A143 P144 H147 Y150 R151 A154 R157 R158
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004048 anthranilate phosphoribosyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0000162 tryptophan biosynthetic process
Cellular Component
GO:0005576 extracellular region
GO:0005829 cytosol
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5bne, PDBe:5bne, PDBj:5bne
PDBsum5bne
PubMed
UniProtP9WFX5|TRPD_MYCTU Anthranilate phosphoribosyltransferase (Gene Name=trpD)

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