Structure of PDB 1h3n Chain A

Receptor sequence
>1h3nA (length=814) Species: 274 (Thermus thermophilus) [Search protein sequence]
MEKYNPHAIEAKWQRFWEEKGFMKAKDLPGGRGKQYVLVMFPYPSGDLHM
GHLKNYTMGDVLARFRRMQGYEVLHPMGWDAFGLPAENAALKFGVHPKDW
TYANIRQAKESLRLMGILYDWDREVTTCEPEYYRWNQWIFLKMWEKGLAY
RAKGLVNWCPKCQTVLANEQVVEGRCWRHEDTPVEKRELEQWYLRITAYA
ERLLKDLEGLNWPEKVKAMQRAWIGRSEGAEILFPVEGKEVRIPVFTTRP
DTLFGATFLVLAPEHPLTLELAAPEKREEVLAYVEAAKRKTEIERQAEGR
EKTGVFLGAYALNPATGERIPIWTADYVLFGYGTGAIMAVPAHDQRDYEF
ARKFGLPIKKVIERPGEPLPEPLERAYEEPGIMVNSGPFDGTESEEGKRK
VIAWLEEKGLGKGRVTYRLRDWLISRQRYWGTPIPMVHCEACGVVPVPEE
ELPVLLPDLKDVEDIRPKGKSPLEAHPEFYETTCPKCGGPAKRDTDTMDT
FFDSSWYYLRYTDPHNDRLPFDPEKANAWMPVDQYIGGVEHAVLHLLYSR
FFTKFLHDLGMVKVEEPFQGLFTQGMVLAWTDFGPVEVEGSVVRLPEPTR
IRLEIPESALSLEDVRKMGAELRPHEDGTLHLWKPAVMSKSKGNGVMVGP
FVKEQGADIARITILFAAPPENEMVWTEEGVQGAWRFLNRIYRRVAEDRE
ALLETSGVFQAEALEGKDRELYGKLHETLKKVTEDLEALRFNTAIAALME
FLNALYEYRKDRPVTPVYRTAIRYYLQMLFPFAPHLAEELWHWFWPDSLF
EAGWPELDEKALEK
3D structure
PDB1h3n The 2A Structure of Leucyl-tRNA Synthetase and its Complex with a Leucyl-Adenylate Analogue
ChainA
Resolution2.0 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 H49 H52 D80 C159 C162 F501 H541 F551 V637 K640
Catalytic site (residue number reindexed from 1) F41 H49 H52 D80 C159 C162 F501 H541 F551 V637 K640
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 LEU A M40 F41 Y43 D80 H541 H545 M40 F41 Y43 D80 H541 H545
BS02 LMS A P42 Y43 G51 H52 N55 Y56 G537 G538 E540 Q574 M576 V577 P42 Y43 G51 H52 N55 Y56 G537 G538 E540 Q574 M576 V577
BS03 ZN A C439 C442 C484 C487 C439 C442 C484 C487
BS04 ZN A C159 C162 C176 H179 C159 C162 C176 H179
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
GO:0046872 metal ion 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:1h3n, PDBe:1h3n, PDBj:1h3n
PDBsum1h3n
PubMed10811626
UniProtQ7SIE4

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