Structure of PDB 2i4o Chain C Binding Site BS01

Receptor Information

>2i4o Chain C (length=441) Species: 1076 (Rhodopseudomonas palustris)

GSHMRLSRFFLPILKENPKEAEIVSHRLMLRAGMLRQEAAGIYAWLPLGH
RVLKKIEQIVREEQNRAGAIELLMPTLQLADLWRESGRYDAYGPEMLRIA
DRHKRELLYGPTNEEMITEIFRAYIKSYKSLPLNLYHIQWKFRDEQRPRF
GVMRGREFLMKDAYSFDVDEAGARKSYNKMFVAYLRTFARMGLKAIPMRA
ETGPIGGDLSHEFIVLAETGESGVYIDRDVLNLPVPDENVDYDGDLTPII
KQWTSVYAATEDVHEPARYESEVPEANRLNTRGIEVGQIFYFGTKYSDSM
KANVTGPDGTDAPIHGGSYGVGVSRLLGAIIEACHDDNGIIWPEAVAPFR
VTILNLKQGDAATDAACDQLYRELSAKGVDVLYDDTDQRAGAKFATADLI
GIPWQIHVGPRGLAEGKVELKRRSDGARENLALADVVARLT

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 2i4o Chain C Residue 439

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2i4o Structures of Two Bacterial Prolyl-tRNA Synthetases with and without a cis-Editing Domain.
• Resolution: 2.4 Å
• Binding residue (original residue number in PDB): E282 Q285
• Binding residue (residue number reindexed from 1): E285 Q288
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): E111 R140 M157 D159 Y161 I246 H312
• Catalytic site (residue number reindexed from 1): E114 R143 M160 D162 Y164 I249 H315
• 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

Biological Process

• GO:0006412 translation
• GO:0006418 tRNA aminoacylation for protein translation
• GO:0006433 prolyl-tRNA aminoacylation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:2i4o, PDBe:2i4o, PDBj:2i4o
• PDBsum: 2i4o
• PubMed: 17027500
• UniProt: Q6N5P6|SYP_RHOPA Proline--tRNA ligase (Gene Name=proS)