Structure of PDB 1h4t Chain D Binding Site BS01

Receptor Information
>1h4t Chain D (length=464) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KGLTPQSQDFSEWYLEVIQKAELADYGPVRGTIVVRPYGYAIWENIQQVL
DRMFKETGHQNAYFPLFIPMSFLFSPELAVVTHAGGEELEEPLAVRPTSE
TVIGYMWSKWIRSWRDLPQLLNQWGNVVRWEMRTRPFLRTSEFLWQEGHT
AHATREEAEEEVRRMLSIYARLAREYAAIPVIEGLKTEKEKFAGAVYTTT
IEALMKDGKALQAGTSHYLGENFARAFDIKFQDRDLQVKYVHTTSWGLSW
RFIGAIIMTHGDDRGLVLPPRLAPIQVVIVPIYKDESRERVLEAAQGLRQ
ALLAQGLRVHLDDRDQHTPGYKFHEWELKGVPFRVELGPKDLEGGQAVLA
SRLGGKETLPLAALPEALPGKLDAFHEELYRRALAFREDHTRKVDTYEAF
KEAVQEGFALAFHCGDKACERLIQEETTATTRCVPFEAEPEEGFCVRCGR
PSAYGKRVVFAKAY
Ligand information
Ligand IDPRO
InChIInChI=1S/C5H9NO2/c7-5(8)4-2-1-3-6-4/h4,6H,1-3H2,(H,7,8)/t4-/m0/s1
InChIKeyONIBWKKTOPOVIA-BYPYZUCNSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1C[C@H](NC1)C(=O)O
CACTVS 3.341OC(=O)[C@@H]1CCCN1
CACTVS 3.341OC(=O)[CH]1CCCN1
OpenEye OEToolkits 1.5.0C1CC(NC1)C(=O)O
ACDLabs 10.04O=C(O)C1NCCC1
FormulaC5 H9 N O2
NamePROLINE
ChEMBLCHEMBL54922
DrugBankDB00172
ZINCZINC000000895360
PDB chain1h4t Chain D Residue 1478 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1h4t A Succession of Substrate Induced Conformational Changes Ensures the Amino Acid Specificity of Thermus Thermophilus Prolyl-tRNA Synthetase: Comparison with Histidyl-tRNA Synthetase
Resolution2.9 Å
Binding residue
(original residue number in PDB)		T111 E113 W158 E160 F205 H230 S258 W259 G260
Binding residue
(residue number reindexed from 1)		T98 E100 W145 E147 F192 H217 S245 W246 G247
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) E113 R142 H162
Catalytic site (residue number reindexed from 1) E100 R129 H149
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:1h4t, PDBe:1h4t, PDBj:1h4t
PDBsum1h4t
PubMed11399074
UniProtQ5SM28|SYP_THET8 Proline--tRNA ligase (Gene Name=proS)

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