Structure of PDB 1h4q Chain B

Receptor sequence
>1h4qB (length=464) Species: 274 (Thermus thermophilus) [Search protein sequence]
KGLTPQSQDFSEWYLEVIQKAELADYGPVRGTIVVRPYGYAIWENIQQVL
DRMFKETGHQNAYFPLFIPMSFLFSPELAVVTHAGGEELEEPLAVRPTSE
TVIGYMWSKWIRSWRDLPQLLNQWGNVVRWEMRTRPFLRTSEFLWQEGHT
AHATREEAEEEVRRMLSIYARLAREYAAIPVIEGLKTEKEKFAGAVYTTT
IEALMKDGKALQAGTSHYLGENFARAFDIKFQDRDLQVKYVHTTSWGLSW
RFIGAIIMTHGDDRGLVLPPRLAPIQVVIVPIYKDESRERVLEAAQGLRQ
ALLAQGLRVHLDDRDQHTPGYKFHEWELKGVPFRVELGPKDLEGGQAVLA
SRLGGKETLPLAALPEALPGKLDAFHEELYRRALAFREDHTRKVDTYEAF
KEAVQEGFALAFHCGDKACERLIQEETTATTRCVPFEAEPEEGFCVRCGR
PSAYGKRVVFAKAY
3D structure
PDB1h4q A Succession of Substrate Induced Conformational Changes Ensures the Amino Acid Specificity of Thermus Thermophilus Prolyl-tRNA Synthetase: Comparison with Histidyl-tRNA Synthetase
ChainB
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
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:1h4q, PDBe:1h4q, PDBj:1h4q
PDBsum1h4q
PubMed11399074
UniProtQ5SM28|SYP_THET8 Proline--tRNA ligase (Gene Name=proS)

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