Structure of PDB 4ycv Chain D

Receptor sequence
>4ycvD (length=479) Species: 5843 (Plasmodium falciparum NF54) [Search protein sequence]
DPRLYFENRSKFIQDQKDKGINPYPHKFERTISIPEFIEKYKDLGNGEHL
EDTILNITGRIMRVSAGQKLRFFDLVGDGEKIQVLANYSFHNHEKGNFAE
CYDKIRRGDIVGIVGFPGKSKGELSIFPKETILLSACLHMLPMKYGLKDT
EIRYRQRYLDLLINESSRHTFVTRTKIINFLRNFLNERGFFEVETPMMNL
INARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGI
DNTHNPEFTSCEFYWAYADYNDLIKWSEDFFSQLVYHLFGTYKISYNKDG
PENQPIEIDFTPPYPKVSIVEEIEKVTNTILEQPFDSNETIEKMINIIKE
HKIELPNPPTAAKLLDQLASHFIENKYNDKPFFIVEHPQIMSPLAKYHRT
KPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAFCTSLEYGLPPTGG
LGLGIDRITMFLTNKNSIKDVILFPTMRP
3D structure
PDB4ycv Structural Basis for Specific Inhibition of tRNA Synthetase by an ATP Competitive Inhibitor.
ChainD
Resolution3.406 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R330 E332 T337 H338 E500 N503 R559
Catalytic site (residue number reindexed from 1) R246 E248 T253 H254 E416 N419 R457
Enzyme Commision number 6.1.1.6: lysine--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 KRS D R330 H338 N339 F342 E500 V501 G556 R559 R246 H254 N255 F258 E416 V417 G454 R457
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004824 lysine-tRNA ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006430 lysyl-tRNA aminoacylation
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:4ycv, PDBe:4ycv, PDBj:4ycv
PDBsum4ycv
PubMed26074468
UniProtW7JP72

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