Structure of PDB 1evl Chain C Binding Site BS02

Receptor Information
>1evl Chain C (length=401) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQ
EVKGPFMMDRVLWEKTGHWDNYKDAMFTTSSENREYCIKPMNCPGHVQIF
NQGLKSYRDLPLRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEE
QIRDEVNGCIRLVYDMYSTFGFEKIVVKLSTRPEKRIGSDEMWDRAEADL
AVALEENNIPFEYQLGEGAFYGPKIEFTLYDCLDRAWQCGTVQLDFSLPS
RLSASYVGEDNERKVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPVQ
VVIMNITDSQSEYVNELTQKLSNAGIRVKADLRNEKIGFKIREHTLRRVP
YMLVCGDKEVESGKVAVRTRRGKDLGSMDVNEVIEKLQQEIRSRSLKQLE
E
Ligand information
Ligand IDTSB
InChIInChI=1S/C14H21N7O8S/c1-5(22)7(15)13(25)20-30(26,27)28-2-6-9(23)10(24)14(29-6)21-4-19-8-11(16)17-3-18-12(8)21/h3-7,9-10,14,22-24H,2,15H2,1H3,(H,20,25)(H2,16,17,18)/t5-,6-,7+,9-,10-,14-/m1/s1
InChIKeyUPVAPSGKXAAHBG-CKTDUXNWSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[CH](O)[CH](N)C(=O)N[S](=O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
CACTVS 3.341C[C@@H](O)[C@H](N)C(=O)N[S](=O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0CC(C(C(=O)NS(=O)(=O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)O)N)O
ACDLabs 10.04O=C(NS(=O)(=O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O)C(N)C(O)C
OpenEye OEToolkits 1.5.0C[C@H]([C@@H](C(=O)NS(=O)(=O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O)N)O
FormulaC14 H21 N7 O8 S
Name5'-O-(N-(L-THREONYL)-SULFAMOYL)ADENOSINE
ChEMBLCHEMBL1163068
DrugBankDB03355
ZINCZINC000015524571
PDB chain1evl Chain C Residue 4002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1evl Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase.
Resolution1.55 Å
Binding residue
(original residue number in PDB)		M332 R363 E365 V376 F379 Q381 D383 H385 Y462 Q479 C480 Q484 S517
Binding residue
(residue number reindexed from 1)		M91 R122 E124 V135 F138 Q140 D142 H144 Y221 Q238 C239 Q243 S276
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) C334 R363 Q381 D383 H385 K465 H511
Catalytic site (residue number reindexed from 1) C93 R122 Q140 D142 H144 K224 H270
Enzyme Commision number 6.1.1.3: threonine--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004829 threonine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006435 threonyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1evl, PDBe:1evl, PDBj:1evl
PDBsum1evl
PubMed10881191
UniProtP0A8M3|SYT_ECOLI Threonine--tRNA ligase (Gene Name=thrS)

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