Structure of PDB 8qc4 Chain B

Receptor sequence
>8qc4B (length=435) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
SSSIPMPAGVNPADLAAELAAVVTESVDEDYLLYECDGQWVLAAGVQAMV
ELDSDELRVIRDGVTRRQQWSGRPGAALGEAVDRLLLETDQAFGWVAFEF
GVHRYGLQQRLAPHTPLARVFSPRTRIMVSEKEIRLFDAGIRHREAIDRL
LATGVREVPQSRSVDVSDDPSGFRRRVAVAVDEIAAGRYHKVILSRCVEV
PFAIDFPLTYRLGRRHNTPVRSFLLQLGGIRALGYSPELVTAVRADGVVI
TEPLAGTRALGRGPAIDRLARDDLESNSKEIVEHAISVRSSLEEITDIAE
PGSAAVIDFMTVRERGSVQHLGSTIRARLDPSSDRMAALEALFPAVTASG
IPKAAGVEAIFRLDECPRGLYSGAVVMLSADGGLDAALTLRAAYQVGGRT
WLRAGAGIIEESEPEREFEETCEKLSTLTPYLVAR
3D structure
PDB8qc4 Structural Study of a New MbtI-Inhibitor Complex: Towards an Optimized Model for Structure-Based Drug Discovery
ChainB
Resolution1.578 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.2.99.21: isochorismate lyase.
5.4.4.2: isochorismate synthase.
5.4.99.5: chorismate mutase.
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 TXR B I207 G270 T271 H334 T361 Y385 L404 R405 A418 G419 K438 I193 G256 T257 H320 T347 Y371 L390 R391 A404 G405 K424
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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Cellular Component
External links
PDB RCSB:8qc4, PDBe:8qc4, PDBj:8qc4
PDBsum8qc4
PubMed38004425
UniProtP9WFX1|MBTI_MYCTU Salicylate synthase (Gene Name=mbtI)

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