Structure of PDB 2g5f Chain B Binding Site BS01

Receptor Information
>2g5f Chain B (length=430) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SIPMPAGVNPADLAAELAAVVTEDEDYLLYECDGQWVLAAGVQAMVELDS
DELRVIRGVTRRQQWSGRPGAALGEAVDRLLLETDQAFGWVAFEFGVHRY
GLQQRLAPHTPLARVFSPRTRIMVSEKEIRLFDAGIRHREAIDRLLATGV
REVPQSRSVDVSDDPSGFRRRVAVAVDEIAAGRYHKVILSRCVEVPFAID
FPLTYRLGRRHNTPVRSFLLQLGGIRALGYSPELVTAVRADGVVITEPLA
GTRALGRGPAIDRLARDDLESNSKEIVEHAISVRSSLEEITDIAEPGSAA
VIDFMTVRERGSVQHLGSTIRARLDPSSDRMAALEALFPAVTASGIPKAA
GVEAIFRLDECPRGLYSGAVVMLSADGGLDAALTLRAAYQVGGRTWLRAG
AGIIEESEPEREFEETCEKLSTLTPYLVAR
Ligand information
Ligand IDPYR
InChIInChI=1S/C3H4O3/c1-2(4)3(5)6/h1H3,(H,5,6)
InChIKeyLCTONWCANYUPML-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CC(=O)C(O)=O
OpenEye OEToolkits 1.7.6CC(=O)C(=O)O
ACDLabs 12.01O=C(C(=O)O)C
FormulaC3 H4 O3
NamePYRUVIC ACID
ChEMBLCHEMBL1162144
DrugBankDB00119
ZINCZINC000001532517
PDB chain2g5f Chain B Residue 2002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2g5f The Structure of MbtI from Mycobacterium tuberculosis, the First Enzyme in the Biosynthesis of the Siderophore Mycobactin, Reveals It To Be a Salicylate Synthase
Resolution1.8 Å
Binding residue
(original residue number in PDB)		A362 Y385 L404 R405 G419 K438
Binding residue
(residue number reindexed from 1)		A343 Y366 L385 R386 G400 K419
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K205 E252 A269 E297 H334 T361 Y385 R405 G421 E434 K438
Catalytic site (residue number reindexed from 1) K186 E233 A250 E278 H315 T342 Y366 R386 G402 E415 K419
Enzyme Commision number 4.2.99.21: isochorismate lyase.
5.4.4.2: isochorismate synthase.
5.4.99.5: chorismate mutase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004106 chorismate mutase activity
GO:0008909 isochorismate synthase activity
GO:0016829 lyase activity
GO:0016833 oxo-acid-lyase activity
GO:0016853 isomerase activity
GO:0043904 isochorismate pyruvate lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0009058 biosynthetic process
GO:0009697 salicylic acid biosynthetic process
GO:0010106 cellular response to iron ion starvation
GO:0019540 catechol-containing siderophore biosynthetic process
GO:0052572 response to host immune response
Cellular Component
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:2g5f, PDBe:2g5f, PDBj:2g5f
PDBsum2g5f
PubMed16923875
UniProtP9WFX1|MBTI_MYCTU Salicylate synthase (Gene Name=mbtI)

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