Structure of PDB 2i4n Chain C

Receptor sequence
>2i4nC (length=442) Species: 1076 (Rhodopseudomonas palustris) [Search protein sequence]
RGSHMRLSRFFLPILKENPKEAEIVSHRLMLRAGMLRQEAAGIYAWLPLG
HRVLKKIEQIVREEQNRAGAIELLMPTLQLADLWRESGRYDAYGPEMLRI
ADRHKRELLYGPTNEEMITEIFRAYIKSYKSLPLNLYHIQWKFRDEQRPR
FGVMRGREFLMKDAYSFDVDEAGARKSYNKMFVAYLRTFARMGLKAIPMR
AETGPIGGDLSHEFIVLAETGESGVYIDRDVLNLPVPDENVDYDGDLTPI
IKQWTSVYAATEDVHEPARYESEVPEANRLNTRGIEVGQIFYFGTKYSDS
MKANVTGPDGTDAPIHGGSYGVGVSRLLGAIIEACHDDNGIIWPEAVAPF
RVTILNLKQGDAATDAACDQLYRELSAKGVDVLYDDTDQRAGAKFATADL
IGIPWQIHVGPRGLAEGKVELKRRSDGARENLALADVVARLT
3D structure
PDB2i4n Structures of Two Bacterial Prolyl-tRNA Synthetases with and without a cis-Editing Domain.
ChainC
Resolution2.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E111 R140 M157 D159 Y161 I246 H312
Catalytic site (residue number reindexed from 1) E115 R144 M161 D163 Y165 I250 H316
Enzyme Commision number 6.1.1.15: proline--tRNA ligase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 5CA C E111 R140 G152 F155 M157 E282 G284 Q285 F287 S315 Y316 G317 G319 R322 E115 R144 G156 F159 M161 E286 G288 Q289 F291 S319 Y320 G321 G323 R326
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2i4n, PDBe:2i4n, PDBj:2i4n
PDBsum2i4n
PubMed17027500
UniProtQ6N5P6|SYP_RHOPA Proline--tRNA ligase (Gene Name=proS)

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