Structure of PDB 6yks Chain A

Receptor sequence
>6yksA (length=813) Species: 485 (Neisseria gonorrhoeae) [Search protein sequence]
MQEHYQPAAIEPAAQKKWDDARISNVSEDASKPKYYCLSMFPYPSGKLHM
GHVRNYTIGDVLSRFKLLNGFNVMQPMGWDAFGMPAENAAMKNNVAPAAW
TYDNIEYMKTQLKSLGFAVDWEREVATCKPEYYRWEQWLFTKLFEKGIVY
RKNGTVNWDPVDQTVLANEQVIDGRGWRSGALIEKREIPMYYFKITDYAE
ELLNDLDKLEHWPEQVKTMQRNWIGKSRGMTVRFAVSDDSKQGLEGDYAK
FLQVYTTRPDTLMGATYVAVAAEHPLATAAAADKPELQAFIAECKAGSVA
EADMATMEKKGVPTGRYVVNPLNGDKLEVWIANYVLWGYGDGAVMAVPAH
DERDFEFAAKYNLPKKQVIAVGDNAFDANRWQEWYGDKENGVLVNSGDLD
GLDFQTAFDAVAAKLQSQGAGEPKTQYRLRDWGISRQRYWGCPIPIVHCE
KCGNVPVPADQLPVVLPENVVPDGMGSPLAKMPEFYETSCPCCGGAAKRE
TDTMDTFIESSWYFFRYMSPKFSDGMVSAESAKYWGAVDQYIGGIEHAIL
HLLYARFFTKLMRDEGLVNVDEPFERLLTQGMVVCETYYRENDKGGKDWI
NPADVELTGRPVSAVLKADGLPVVISGTEKMSKSKNNGVDPQELINAYGA
DTARLFMMFAAPPEQSLEWSDSGVEGAHRFLRRLWRTVYEYLKQGGAVKA
FAGNQDGLSKELKDLRHKLHSTTAKVSDDYGRRQQFNTAIAAVMELLNQY
DKTDTGSEQGRAVAQEVLEAAVRLLWPIVPHICETLWSELNGAKLWEAGW
PTVDEAALVKSEI
3D structure
PDB6yks Synthesis and structure-activity studies of novel anhydrohexitol-based Leucyl-tRNA synthetase inhibitors.
ChainA
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F41 D80 F507 H547 F557 K634 K637
Catalytic site (residue number reindexed from 1) F41 D80 F507 H547 F557 K630 K633
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 OVT A M40 F41 P42 Y43 H49 H52 N55 Y56 D80 S510 G543 G544 E546 H547 H551 M582 V583 K634 M635 M40 F41 P42 Y43 H49 H52 N55 Y56 D80 S510 G543 G544 E546 H547 H551 M582 V583 K630 M631 MOAD: Ki=108.35nM
BS02 ZN A C449 C452 C490 C493 C449 C452 C490 C493
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0002161 aminoacyl-tRNA editing activity
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004823 leucine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006429 leucyl-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:6yks, PDBe:6yks, PDBj:6yks
PDBsum6yks
PubMed33248851
UniProtQ5FAJ3|SYL_NEIG1 Leucine--tRNA ligase (Gene Name=leuS)

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