Structure of PDB 2rjs Chain A Binding Site BS02

Receptor Information
>2rjs Chain A (length=526) Species: 1908 (Streptomyces globisporus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PVSVDGETLTVEAVRRVAEERATVDVPAESIAKAQKSREIFEGIAEQNIP
IYGVTTGYGEMIYMQVDKSKEVELQTNLVRSHSAGVGPLFAEDEARAIVA
ARLNTLAKGHSAVRPIILERLAQYLNEGITPAIPEIGSLGGDLAPLSHVA
STLIGEGYVLRDGRPVETAQVLAERGIEPLELRFKEGLALINGTSGMTGL
GSLVVGRALEQAQQAEIVTALLIEAVRGSTSPFLAEGHDIARPHEGQIDT
AANMRALMRGSGLTVEHADLRRELQKDKEAGKDVQRSEIYLQKAYSLRAI
PQVVGAVRDTLYHARHKLRIELNSANDNPLFFEGKEIFHGANFHGQPIAF
AMDFVTIALTQLGVLAERQINRVLNRHLSYGLPEFLVSGDPGLHSGFAGA
QYPATALVAENRTIGPASTQSVPSNGDNQDVVSMGLISARNARRVLSNNN
KILAVEYLAAAQAVDISGRFDGLSPAAKATYEAVRRLVPTLGVDRYMADD
IELVADALSRGEFLRAIARETDIQLR
Ligand information
Ligand ID296
InChIInChI=1S/C10H11F2NO3/c1-16-7-4-2-6(3-5-7)8(13)10(11,12)9(14)15/h2-5,8H,13H2,1H3,(H,14,15)/t8-/m1/s1
InChIKeyLSCGPDBHPYAPAB-MRVPVSSYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341COc1ccc(cc1)[C@@H](N)C(F)(F)C(O)=O
OpenEye OEToolkits 1.5.0COc1ccc(cc1)[C@H](C(C(=O)O)(F)F)N
ACDLabs 10.04O=C(O)C(F)(F)C(c1ccc(OC)cc1)N
OpenEye OEToolkits 1.5.0COc1ccc(cc1)C(C(C(=O)O)(F)F)N
CACTVS 3.341COc1ccc(cc1)[CH](N)C(F)(F)C(O)=O
FormulaC10 H11 F2 N O3
Name(3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid
ChEMBLCHEMBL255510
DrugBank
ZINCZINC000016052537
PDB chain2rjs Chain B Residue 1001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2rjs Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		Y308 R311
Binding residue
(residue number reindexed from 1)		Y295 R298
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y63 G70 H93 N205 Y308 R311 F356 Q442
Catalytic site (residue number reindexed from 1) Y52 G59 H82 N192 Y295 R298 F343 Q429
Enzyme Commision number 4.3.1.23: tyrosine ammonia-lyase.
5.4.3.6: tyrosine 2,3-aminomutase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004397 histidine ammonia-lyase activity
GO:0016829 lyase activity
GO:0016841 ammonia-lyase activity
GO:0016853 isomerase activity
GO:0050368 L-tyrosine 2,3-aminomutase activity
GO:0052883 tyrosine ammonia-lyase activity
Biological Process
GO:0006548 L-histidine catabolic process
GO:0009403 toxin biosynthetic process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2rjs, PDBe:2rjs, PDBj:2rjs
PDBsum2rjs
PubMed18078753
UniProtQ8GMG0|TAM_STRGL MIO-dependent tyrosine 2,3-aminomutase

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