Structure of PDB 1jzs Chain A

Receptor sequence
>1jzsA (length=821) Species: 274 (Thermus thermophilus) [Search protein sequence]
MFKEVGEPNFPKLEEEVLAFWKREKIFQKSVENRKGGPRYTVYEGPPTAN
GLPHVGHAQARSYKDLFPRYKTMRGYYAPRRAGWDTHGLPVELEVEKKLG
LKSKREIEAYGIERFNQACRESVFTYEKEWEAFTERIAYWVDLEDAYATL
EPTYIESIWWSLKNLFDRGLLYRDHKVVPYCPRCGTPLSSHEVALGYKEI
QDPSVYVRFPLKEPKKLGLEKASLLIWTTTPWTLPGNVAAAVHPEYTYAA
FQVGDEALILEEGLGRKLLGEGTQVLKTFPGKALEGLPYTPPYPQALEKG
YFVVLADYVSQEDGTGIVHQAPAFGAEDLETARVYGLPLLKTVDEEGKLL
VEPFKGLYFREANRAILRDLRGRGLLFKEESYLHSYPHCWRCSTPLMYYA
TESWFIKNTLFKDELIRNNQEIHWVPPHIKEGRYGEWLKNLVDWALSRNR
YWGTPLPIWVCQACGKEEAIGSFQELKARATKPLPEPFDPHRPYVDQVEL
ACACGGTMRRVPYVIDVWYDSGAMPFASLHYPFEHEEVFRESFPADFIAE
GIDQTRGWFNSLHQLGVMLFGSIAFKNVICHGLILDEKGQKMSKSKGNVV
DPWDIIRKFGADALRWYIYVSAPPEADRRFGPNLVRETVRDYFLTLWNVY
SFFVTYANLDRPDLKNPPPPEKRPEMDRWLLARMQDLIQRVTEALEAYDP
TTSARALRDFVVEDLSQWYVRRNRRRFWKNEDALDREAAYATLYEALVLV
ATLAAPFTPFLAEVLWQNLVRSVRLEAKESVHLADWPEADPALADEALVA
QMRAVLKVVDLARAARAKSGV
3D structure
PDB1jzs Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) P46 H54 H57 D85 W518 Q554 W558 K591 K594
Catalytic site (residue number reindexed from 1) P46 H54 H57 D85 W518 Q554 W558 K591 K594
Enzyme Commision number 6.1.1.5: isoleucine--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 ZN A C181 C184 C389 C181 C184 C389
BS02 ZN A C464 G465 C504 C464 G465 C504
BS03 MRC A P46 G56 E550 G551 D553 Q554 P46 G56 E550 G551 D553 Q554 MOAD: Ki=0.25uM
PDBbind-CN: -logKd/Ki=6.60,Ki=0.25uM
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0002161 aminoacyl-tRNA editing activity
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004822 isoleucine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006428 isoleucyl-tRNA aminoacylation

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Molecular Function
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Biological Process
External links
PDB RCSB:1jzs, PDBe:1jzs, PDBj:1jzs
PDBsum1jzs
PubMed11584022
UniProtP56690|SYI_THET8 Isoleucine--tRNA ligase (Gene Name=ileS)

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