Structure of PDB 2j3m Chain A

Receptor sequence
>2j3mA (length=554) Species: 1351 (Enterococcus faecalis) [Search protein sequence]
MKQSKMLIPTLEVLSHQILLRAGYIRQVAAGIYSYLPLANRVLEKLKTIM
REEFEKIDAVEMLMPALLPAELWKESGRYETYGPNLYRLKDRNDRDYILG
PTHEETFTELIRDEINSYKRLPLNLYQIQTKYRDEKRSRSGLLRGREFIM
KDGYSFHADEASLDQSYRDYEKAYSRIFERCGLEFRAIIGDGGKDSKEFM
AISEIGEDTICYSTESDYAANLEMATSLYTPKKSHETQLDLEKIATPEVG
TIAEVANFFEVEPQRIIKSVLFIADEEPVMVLVRGDHDVNDVKLKNFLGA
DFLDEATEEDARRVLGAGFGSIGPVNVSEDVKIYADLAVQDLANAIVGAN
EDGYHLTNVNPDRDFQPISYEDLRFVQEGDPSPDGNGVLAFTKGIEIGHI
FKLGTRYSDAMGATVLDENGREKSVIMGCYGIGVSRLLSAIVEQNADERG
INWPTGIAPFDLHVVQMNVKDEYQTKLSQEVEAMMTEAGYEVLVDDRNER
AGVKFADADLIGCPIRITVGKKAVDGVVEVKIKRTGEMLEVRKEELESTL
SILM
3D structure
PDB2j3m Structures of Two Bacterial Prolyl-tRNA Synthetases with and without a Cis-Editing Domain.
ChainA
Resolution2.3 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 V336 I437
Catalytic site (residue number reindexed from 1) E104 R133 M150 D152 Y154 V325 I426
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 ATP A R140 E142 R151 G152 F155 M157 E407 I408 G409 H410 G444 R447 R133 E135 R144 G145 F148 M150 E396 I397 G398 H399 G433 R436
BS02 PRI A T109 E111 M157 D159 Y161 F412 C440 Y441 G442 T102 E104 M150 D152 Y154 F401 C429 Y430 G431
BS03 MN A E407 H410 E396 H399
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0002161 aminoacyl-tRNA editing activity
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004827 proline-tRNA ligase activity
GO:0005524 ATP binding
GO:0016740 transferase activity
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006433 prolyl-tRNA aminoacylation
GO:0106074 aminoacyl-tRNA metabolism involved in translational fidelity
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:2j3m, PDBe:2j3m, PDBj:2j3m
PDBsum2j3m
PubMed17027500
UniProtQ831W7|SYP_ENTFA Proline--tRNA ligase (Gene Name=proS)

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