Structure of PDB 4x5b Chain B

Receptor sequence
>4x5bB (length=346) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
PSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKAP
TADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMAAI
VVAAAGVPVVKHGNRAASSLSGGADTLEALGVRIDLGPDLVARSLAEVGI
GFCFAPRFHPSYRHAAAVLREIGVPTVFNLLGPLTNPARPRAGLIGCAFA
DLAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLTF
DPAGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGAI
VAHAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQI
3D structure
PDB4x5b Structures of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Variants Reveal the Conformational Changes That Facilitate Delivery of the Substrate to the Active Site.
ChainB
Resolution2.47 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 PRP B G107 G109 G110 N117 S119 T120 N138 A140 A141 S142 S143 G146 G83 G85 G86 N93 S95 T96 N114 A116 A117 S118 S119 G122
BS02 MG B G107 S119 E252 G83 S95 E228
BS03 MG B D251 E252 D227 E228
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:4x5b, PDBe:4x5b, PDBj:4x5b
PDBsum4x5b
PubMed26356348
UniProtP9WFX5|TRPD_MYCTU Anthranilate phosphoribosyltransferase (Gene Name=trpD)

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