Structure of PDB 1h4s Chain B Binding Site BS03

Receptor Information
>1h4s Chain B (length=473) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KGLTPQSQDFSEWYLEVIQKAELADYGPVRGTIVVRPYGYAIWENIQQVL
DRMFKETGHQNAYFPLFIPMSFLRKEAEHVEGFSPELAVVTHAGGEELEE
PLAVRPTSETVIGYMWSKWIRSWRDLPQLLNQWGNVVRWEMRTRPFLRTS
EFLWQEGHTAHATREEAEEEVRRMLSIYARLAREYAAIPVIEGLKTEKEK
FAGAVYTTTIEALMKDGKALQAGTSHYLGENFARAFDIKFQDRDLQVKYV
HTTSWGLSWRFIGAIIMTHGDDRGLVLPPRLAPIQVVIVPIYKDESRERV
LEAAQGLRQALLAQGLRVHLDDRDQHTPGYKFHEWELKGVPFRVELGPKD
LEGGQAVLASRLGGKETLPLAALPEALPGKLDAFHEELYRRALAFREDHT
RKVDTYEAFKEAVQEGFALAFHCGDKACERLIQEETTATTRCVPFEAEPE
EGFCVRCGRPSAYGKRVVFAKAY
Ligand information
Ligand IDP5A
InChIInChI=1S/C15H21N7O7S/c16-12-9-13(19-5-18-12)22(6-20-9)15-11(24)10(23)8(29-15)4-28-30(26,27)21-14(25)7-2-1-3-17-7/h5-8,10-11,15,17,23-24H,1-4H2,(H,21,25)(H2,16,18,19)/t7-,8+,10+,11+,15+/m0/s1
InChIKeyLKVJEMXWEODCAY-JVEUSOJLSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[S](=O)(=O)NC(=O)[CH]4CCCN4)[CH](O)[CH]3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[S](=O)(=O)NC(=O)[C@@H]4CCCN4)[C@@H](O)[C@H]3O
ACDLabs 10.04O=C(NS(=O)(=O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O)C4NCCC4
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COS(=O)(=O)NC(=O)[C@@H]4CCCN4)O)O)N
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COS(=O)(=O)NC(=O)C4CCCN4)O)O)N
FormulaC15 H21 N7 O7 S
Name'5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE
ChEMBLCHEMBL1163086
DrugBankDB02510
ZINCZINC000013542769
PDB chain1h4s Chain B Residue 1478 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1h4s A Succession of Substrate Induced Conformational Changes Ensures the Amino Acid Specificity of Thermus Thermophilus Prolyl-tRNA Synthetase: Comparison with Histidyl-tRNA Synthetase
Resolution2.85 Å
Binding residue
(original residue number in PDB)		T111 E113 R142 E144 L151 R152 T153 F156 W158 E160 F205 Q225 G227 T228 H230 S258 W259 G260 S262 R264
Binding residue
(residue number reindexed from 1)		T107 E109 R138 E140 L147 R148 T149 F152 W154 E156 F201 Q221 G223 T224 H226 S254 W255 G256 S258 R260
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) E113 R142 H162
Catalytic site (residue number reindexed from 1) E109 R138 H158
Enzyme Commision number 6.1.1.15: proline--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004827 proline-tRNA ligase activity
GO:0005524 ATP binding
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006433 prolyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0017101 aminoacyl-tRNA synthetase multienzyme complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1h4s, PDBe:1h4s, PDBj:1h4s
PDBsum1h4s
PubMed11399074
UniProtQ5SM28|SYP_THET8 Proline--tRNA ligase (Gene Name=proS)

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