Structure of PDB 2i4n Chain A

Receptor sequence
>2i4nA (length=441) Species: 1076 (Rhodopseudomonas palustris) [Search protein sequence]
GSHMRLSRFFLPILKENPKEAEIVSHRLMLRAGMLRQEAAGIYAWLPLGH
RVLKKIEQIVREEQNRAGAIELLMPTLQLADLWRESGRYDAYGPEMLRIA
DRHKRELLYGPTNEEMITEIFRAYIKSYKSLPLNLYHIQWKFRDEQRPRF
GVMRGREFLMKDAYSFDVDEAGARKSYNKMFVAYLRTFARMGLKAIPMRA
ETGPIGGDLSHEFIVLAETGESGVYIDRDVLNLPVPDENVDYDGDLTPII
KQWTSVYAATEDVHEPARYESEVPEANRLNTRGIEVGQIFYFGTKYSDSM
KANVTGPDGTDAPIHGGSYGVGVSRLLGAIIEACHDDNGIIWPEAVAPFR
VTILNLKQGDAATDAACDQLYRELSAKGVDVLYDDTDQRAGAKFATADLI
GIPWQIHVGPRGLAEGKVELKRRSDGARENLALADVVARLT
3D structure
PDB2i4n Structures of Two Bacterial Prolyl-tRNA Synthetases with and without a cis-Editing Domain.
ChainA
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) E114 R143 M160 D162 Y164 I249 H315
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 A T109 E111 R140 E142 F155 M157 D159 E282 V283 G284 Q285 S315 Y316 G317 G319 R322 T112 E114 R143 E145 F158 M160 D162 E285 V286 G287 Q288 S318 Y319 G320 G322 R325
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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