Structure of PDB 1hc7 Chain A Binding Site BS01

Receptor Information
>1hc7 Chain A (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 IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1hc7 Chain A Residue 490 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1hc7 A Succession of Substrate Induced Conformational Changes Ensures the Amino Acid Specificity of Thermus Thermophilus Prolyl-tRNA Synthetase: Comparison with Histidyl-tRNA Synthetase
Resolution2.43 Å
Binding residue
(original residue number in PDB)		C427 C432 C458 C461
Binding residue
(residue number reindexed from 1)		C414 C419 C445 C448
Annotation score1
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1hc7, PDBe:1hc7, PDBj:1hc7
PDBsum1hc7
PubMed11399074
UniProtQ5SM28|SYP_THET8 Proline--tRNA ligase (Gene Name=proS)

[Back to BioLiP]