Structure of PDB 2i4o Chain B

Receptor sequence
>2i4oB (length=441) Species: 1076 (Rhodopseudomonas palustris) [Search protein sequence]
GSHMRLSRFFLPILKENPKEAEIVSHRLMLRAGMLRQEAAGIYAWLPLGH
RVLKKIEQIVREEQNRAGAIELLMPTLQLADLWRESGRYDAYGPEMLRIA
DRHKRELLYGPTNEEMITEIFRAYIKSYKSLPLNLYHIQWKFRDEQRPRF
GVMRGREFLMKDAYSFDVDEAGARKSYNKMFVAYLRTFARMGLKAIPMRA
ETGPIGGDLSHEFIVLAETGESGVYIDRDVLNLPVPDENVDYDGDLTPII
KQWTSVYAATEDVHEPARYESEVPEANRLNTRGIEVGQIFYFGTKYSDSM
KANVTGPDGTDAPIHGGSYGVGVSRLLGAIIEACHDDNGIIWPEAVAPFR
VTILNLKQGDAATDAACDQLYRELSAKGVDVLYDDTDQRAGAKFATADLI
GIPWQIHVGPRGLAEGKVELKRRSDGARENLALADVVARLT
3D structure
PDB2i4o Structures of Two Bacterial Prolyl-tRNA Synthetases with and without a cis-Editing Domain.
ChainB
Resolution2.4 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 MG B E282 Q285 E285 Q288
BS02 ATP B R140 R151 G152 F155 M157 E282 V283 G284 G319 R322 R143 R154 G155 F158 M160 E285 V286 G287 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:2i4o, PDBe:2i4o, PDBj:2i4o
PDBsum2i4o
PubMed17027500
UniProtQ6N5P6|SYP_RHOPA Proline--tRNA ligase (Gene Name=proS)

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