Structure of PDB 1h4q Chain A Binding Site BS01

Receptor Information
>1h4q Chain A (length=465) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KGLTPQSQDFSEWYLEVIQKAELADYGPVRGTIVVRPYGYAIWENIQQVL
DRMFKETGHQNAYFPLFIPMSFLRFSPELAVVTHAGGEELEEPLAVRPTS
ETVIGYMWSKWIRSWRDLPQLLNQWGNVVRWEMRTRPFLRTSEFLWQEGH
TAHATREEAEEEVRRMLSIYARLAREYAAIPVIEGLKTEKEKFAGAVYTT
TIEALMKDGKALQAGTSHYLGENFARAFDIKFQDRDLQVKYVHTTSWGLS
WRFIGAIIMTHGDDRGLVLPPRLAPIQVVIVPIYKDESRERVLEAAQGLR
QALLAQGLRVHLDDRDQHTPGYKFHEWELKGVPFRVELGPKDLEGGQAVL
ASRLGGKETLPLAALPEALPGKLDAFHEELYRRALAFREDHTRKVDTYEA
FKEAVQEGFALAFHCGDKACERLIQEETTATTRCVPFEAEPEEGFCVRCG
RPSAYGKRVVFAKAY
Ligand information
>1h4q Chain T (length=67) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ggaguagcgcagcccgguagcgcaccucguucgggacgaggggggcgcug
guucagauccagucucc
<<<<..<<<<.........>>>>.<<<<<<.....>>>>>>.....<<<<
<.......>>>>>>>>>
Receptor-Ligand Complex Structure
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PDB1h4q A Succession of Substrate Induced Conformational Changes Ensures the Amino Acid Specificity of Thermus Thermophilus Prolyl-tRNA Synthetase: Comparison with Histidyl-tRNA Synthetase
Resolution3.0 Å
Binding residue
(original residue number in PDB)		S126 W127 R128 Q245 R247 L249
Binding residue
(residue number reindexed from 1)		S114 W115 R116 Q233 R235 L237
Enzymatic activity
Catalytic site (original residue number in PDB) E113 R142 H162
Catalytic site (residue number reindexed from 1) E101 R130 H150
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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Biological Process
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Cellular Component
External links
PDB RCSB:1h4q, PDBe:1h4q, PDBj:1h4q
PDBsum1h4q
PubMed11399074
UniProtQ5SM28|SYP_THET8 Proline--tRNA ligase (Gene Name=proS)

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