Structure of PDB 2j3m Chain B

Receptor sequence
>2j3mB (length=558) Species: 1351 (Enterococcus faecalis) [Search protein sequence]
MKQSKMLIPTLEVLSHQILLRAGYIRQVAAGIYSYLPLANRVLEKLKTIM
REEFEKIDAVEMLMPALLPAELWKESGRYETYGPNLYRLKDRNDRDYILG
PTHEETFTELIRDEINSYKRLPLNLYQIQTKYRDEKRSRSGLLRGREFIM
KDGYSFHADEASLDQSYRDYEKAYSRIFERCGLEFRAIIGDGGAMGGKDS
KEFMAISEIGEDTICYSTESDYAANLEMATSLYTPKKSHETQLDLEKIAT
PEVGTIAEVANFFEVEPQRIIKSVLFIADEEPVMVLVRGDHDVNDVKLKN
FLGADFLDEATEEDARRVLGAGFGSIGPVNVSEDVKIYADLAVQDLANAI
VGANEDGYHLTNVNPDRDFQPISYEDLRFVQEGDPSPDGNGVLAFTKGIE
IGHIFKLGTRYSDAMGATVLDENGREKSVIMGCYGIGVSRLLSAIVEQNA
DERGINWPTGIAPFDLHVVQMNVKDEYQTKLSQEVEAMMTEAGYEVLVDD
RNERAGVKFADADLIGCPIRITVGKKAVDGVVEVKIKRTGEMLEVRKEEL
ESTLSILM
3D structure
PDB2j3m Structures of Two Bacterial Prolyl-tRNA Synthetases with and without a Cis-Editing Domain.
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 V329 I430
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 B R140 E142 R151 G152 F155 M157 E407 I408 G409 H410 G442 G444 R447 R133 E135 R144 G145 F148 M150 E400 I401 G402 H403 G435 G437 R440
BS02 PRI B T109 R140 M157 D159 Y161 C440 Y441 G442 T102 R133 M150 D152 Y154 C433 Y434 G435
BS03 MN B E407 H410 E400 H403
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2j3m, PDBe:2j3m, PDBj:2j3m
PDBsum2j3m
PubMed17027500
UniProtQ831W7|SYP_ENTFA Proline--tRNA ligase (Gene Name=proS)

[Back to BioLiP]