Structure of PDB 6lpf Chain B

Receptor sequence
>6lpfB (length=1006) Species: 9606 (Homo sapiens) [Search protein sequence]
TAKVDFLKKIEKEIQQKWDTERVFEVNASNLEKQTSKGKYFVTFPYPYMN
GRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKR
EIELYGCPPDFPKYQWGIMKSLGLSDEEIVKFSEAEHWLDYFPPLAIQDL
KRMGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFGKRYTIYSP
KDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEPYPSKLSGLKGKNIFLVAA
TLRPETMFGQTNCWVRPDMKYIGFETVNGDIFICTQKAARNMSYQGFTKD
NGVVPVVKELMGEEILGASLSAPLTSYKVIYVLPMLTIKEDKGTGVVTSV
PSDSPDDIAALRDLKKKQALRAKYGIRDDMVLPFEPVPVIEIPGFGNLSA
VTICDELKIQSQNDREKLAEAKEKIYLKGFYEGIMLVDGFKGQKVQDVKK
TIQKKMIDAGDALIYMEPEKQVMSRSSDECVVALCDQWYLDYGEENWKKQ
TSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIE
SLSDSTIYMAFYTVAHLLQGGNLHGQAESPLGIRPQQMTKEVWDYVFFKE
APFPKTQIAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAM
WPEQSDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLA
LADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMVANWDSLRSGPASTF
NDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELAVEG
MHRELVFRFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAGPVN
EVLIHSSQYLMEVTHDLRLRLKNYMMPSHCTIYVAKNYPPWQHTTLSVLR
KHFEANNGKLPDNKVIASELGSMPELKKYMKKVMPFVAMIKENLEKMGPR
ILDLQLEFDEKAVLMENIVYLTNSLELEHIEVKFASEAEDKIREDCCPGK
PLNVFR
3D structure
PDB6lpf Molecular basis of the multifaceted functions of human leucyl-tRNA synthetase in protein synthesis and beyond.
ChainB
Resolution2.49 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y52 H91 V638 L677 Y687 K716 K719
Catalytic site (residue number reindexed from 1) Y46 H85 V596 L635 Y645 K674 K677
Enzyme Commision number 6.1.1.4: leucine--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 LSS B F50 P51 Y52 P53 Y54 G62 H63 S66 H91 S673 G674 H681 H709 L710 F44 P45 Y46 P47 Y48 G56 H57 S60 H85 S631 G632 H639 H667 L668
BS02 VRT B T293 L294 T298 I380 K381 K384 V389 D399 T251 L252 T256 I338 K339 K342 V347 D357
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0002161 aminoacyl-tRNA editing activity
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004819 glutamine-tRNA ligase activity
GO:0004823 leucine-tRNA ligase activity
GO:0005096 GTPase activator activity
GO:0005515 protein binding
GO:0005524 ATP binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006425 glutaminyl-tRNA aminoacylation
GO:0006429 leucyl-tRNA aminoacylation
GO:0008361 regulation of cell size
GO:0032008 positive regulation of TOR signaling
GO:0034198 cellular response to amino acid starvation
GO:0043547 positive regulation of GTPase activity
GO:0071230 cellular response to amino acid stimulus
GO:0071233 cellular response to L-leucine
GO:0106074 aminoacyl-tRNA metabolism involved in translational fidelity
GO:1904263 positive regulation of TORC1 signaling
GO:1990253 cellular response to leucine starvation
Cellular Component
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0005783 endoplasmic reticulum
GO:0005829 cytosol
GO:0012505 endomembrane system
GO:0016604 nuclear body
GO:0017101 aminoacyl-tRNA synthetase multienzyme complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6lpf, PDBe:6lpf, PDBj:6lpf
PDBsum6lpf
PubMed32232361
UniProtQ9P2J5|SYLC_HUMAN Leucine--tRNA ligase, cytoplasmic (Gene Name=LARS1)

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