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Structure of PDB 1h4q Chain B Binding Site BS02

Receptor Information

>1h4q Chain B (length=464) Species: 274 (Thermus thermophilus)

KGLTPQSQDFSEWYLEVIQKAELADYGPVRGTIVVRPYGYAIWENIQQVL
DRMFKETGHQNAYFPLFIPMSFLFSPELAVVTHAGGEELEEPLAVRPTSE
TVIGYMWSKWIRSWRDLPQLLNQWGNVVRWEMRTRPFLRTSEFLWQEGHT
AHATREEAEEEVRRMLSIYARLAREYAAIPVIEGLKTEKEKFAGAVYTTT
IEALMKDGKALQAGTSHYLGENFARAFDIKFQDRDLQVKYVHTTSWGLSW
RFIGAIIMTHGDDRGLVLPPRLAPIQVVIVPIYKDESRERVLEAAQGLRQ
ALLAQGLRVHLDDRDQHTPGYKFHEWELKGVPFRVELGPKDLEGGQAVLA
SRLGGKETLPLAALPEALPGKLDAFHEELYRRALAFREDHTRKVDTYEAF
KEAVQEGFALAFHCGDKACERLIQEETTATTRCVPFEAEPEEGFCVRCGR
PSAYGKRVVFAKAY

Ligand information

• Ligand ID: ATP
• InChI: InChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
• InChIKey: ZKHQWZAMYRWXGA-KQYNXXCUSA-N
• SMILES:
  OpenEye OEToolkits 1.5.0: c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
  CACTVS 3.341: Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
  ACDLabs 10.04: O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
  OpenEye OEToolkits 1.5.0: c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N
  CACTVS 3.341: Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
• Formula: C10 H16 N5 O13 P3
• Name: ADENOSINE-5'-TRIPHOSPHATE
• ChEMBL: CHEMBL14249
• DrugBank: DB00171
• ZINC: ZINC000004261765
• PDB chain: 1h4q Chain B Residue 1478

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1h4q A Succession of Substrate Induced Conformational Changes Ensures the Amino Acid Specificity of Thermus Thermophilus Prolyl-tRNA Synthetase: Comparison with Histidyl-tRNA Synthetase
• Resolution: 3.0 Å
• Binding residue (original residue number in PDB): R142 R152 F156 Q225 T228 S262 R264
• Binding residue (residue number reindexed from 1): R129 R139 F143 Q212 T215 S249 R251
• Annotation score: 5

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

External links

• PDB: RCSB:1h4q, PDBe:1h4q, PDBj:1h4q
• PDBsum: 1h4q
• PubMed: 11399074
• UniProt: Q5SM28|SYP_THET8 Proline--tRNA ligase (Gene Name=proS)

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