Structure of PDB 2v0c Chain A

Receptor sequence
>2v0cA (length=810) Species: 274 (Thermus thermophilus) [Search protein sequence]
MEKYNPHAIEAKWQRFWEEKGFMKAKDLPGKQYVLVMFPYPSGDLHMGHL
KNYTMGDVLARFRRMQGYEVLHPMGWDAFGLPAENAALKFGVHPKDWTYA
NIRQAKESLRLMGILYDWDREVTTCEPEYYRWNQWIFLKMWEKGLAYRAK
GLVNWCPKCQTVLANEQVVEGRCWRHEDTPVEKRELEQWYLRITAYAERL
LKDLEGLNWPEKVKAMQRAWIGRSEGAEILFPVEGKEVRIPVFTTRPDTL
FGATFLVLAPEHPLTLELAAPEKREEVLAYVEAAKRKTEIERQAEGREKT
GVFLGAYALNPATGERIPIWTADYVLFGYGTGAIMAVPAHDQRDYEFARK
FGLPIKKVIERPGEPLPEPLERAYEEPGIMVNSGPFDGTESEEGKRKVIA
WLEEKGLGKGRVTYRLRDWLISRQRYWGTPIPMVHCEACGVVPVPEEELP
VLLPDLKDVEDIRPKGKSPLEAHPEFYETTCPKCGGPAKRDTDTMDTFFD
SSWYYLRYTDPHNDRLPFDPEKANAWMPVDQYIGGVEHAVLHLLYSRFFT
KFLHDLGMVKVEEPFQGLFTQGMVLAWTDFGPVEVEGSVVRLPEPTRIRL
EIPESALSLEDVRKMGAELRPHEDGTLHLWKPAVMSKSKGNGVMVGPFVK
EQGADIARITILFAAPPENEMVWTEEGVQGAWRFLNRIYRRVAEDREALL
ETSGVFQAEALEGKDRELYGKLHETLKKVTEDLEALRFNTAIAALMEFLN
ALYEYRKDRPVTPVYRTAIRYYLQMLFPFAPHLAEELWHWFWPDSLFEAG
WPELDEKALE
3D structure
PDB2v0c An Antifungal Agent Inhibits an Aminoacyl-tRNA Synthetase by Trapping tRNA in the Editing Site.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) F38 H46 H49 D77 C156 C159 F498 H538 F548 V634 K637
Enzyme Commision number 6.1.1.4: leucine--tRNA ligase.
Interaction with ligand
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2v0c, PDBe:2v0c, PDBj:2v0c
PDBsum2v0c
PubMed17588934
UniProtQ7SIE4

[Back to BioLiP]