Structure of PDB 2j3m Chain A Binding Site BS03

Receptor Information
>2j3m Chain A (length=554) Species: 1351 (Enterococcus faecalis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKQSKMLIPTLEVLSHQILLRAGYIRQVAAGIYSYLPLANRVLEKLKTIM
REEFEKIDAVEMLMPALLPAELWKESGRYETYGPNLYRLKDRNDRDYILG
PTHEETFTELIRDEINSYKRLPLNLYQIQTKYRDEKRSRSGLLRGREFIM
KDGYSFHADEASLDQSYRDYEKAYSRIFERCGLEFRAIIGDGGKDSKEFM
AISEIGEDTICYSTESDYAANLEMATSLYTPKKSHETQLDLEKIATPEVG
TIAEVANFFEVEPQRIIKSVLFIADEEPVMVLVRGDHDVNDVKLKNFLGA
DFLDEATEEDARRVLGAGFGSIGPVNVSEDVKIYADLAVQDLANAIVGAN
EDGYHLTNVNPDRDFQPISYEDLRFVQEGDPSPDGNGVLAFTKGIEIGHI
FKLGTRYSDAMGATVLDENGREKSVIMGCYGIGVSRLLSAIVEQNADERG
INWPTGIAPFDLHVVQMNVKDEYQTKLSQEVEAMMTEAGYEVLVDDRNER
AGVKFADADLIGCPIRITVGKKAVDGVVEVKIKRTGEMLEVRKEELESTL
SILM
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain2j3m Chain A Residue 1567 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2j3m Structures of Two Bacterial Prolyl-tRNA Synthetases with and without a Cis-Editing Domain.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		E407 H410
Binding residue
(residue number reindexed from 1)		E396 H399
Annotation score1
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.
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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