Structure of PDB 1zvw Chain A Binding Site BS02
Receptor Information
>1zvw Chain A (length=346) Species:
1773
(Mycobacterium tuberculosis) [
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PSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPAQIAAFAVAMTMKAP
TADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLSTMAAI
VVAAAGVPVVKHGNRAASSLSGGADTLEALGVRIDLGPDLVARSLAEVGI
GFCFAPRFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAFA
DLAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLTF
DPAGFGFARAQLDQLAGGDAQANAAAVRAVLGGARGPVRDAVVLNAAGAI
VAHAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLLARWVRFGRQI
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
1zvw Chain A Residue 6001 [
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Receptor-Ligand Complex Structure
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PDB
1zvw
The Crystal Structure of TrpD, a Metabolic Enzyme Essential for Lung Colonization by Mycobacterium tuberculosis, in Complex with its Substrate Phosphoribosylpyrophosphate.
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
D251 E252
Binding residue
(residue number reindexed from 1)
D227 E228
Annotation score
1
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.
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:1zvw
,
PDBe:1zvw
,
PDBj:1zvw
PDBsum
1zvw
PubMed
16337227
UniProt
P9WFX5
|TRPD_MYCTU Anthranilate phosphoribosyltransferase (Gene Name=trpD)
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