Structure of PDB 2v0g Chain D

Receptor sequence

>2v0gD (length=876) Species: 274 (Thermus thermophilus)

MEKYNPHAIEAKWQRFWEEKGFMKAKDLPGGRGKQYVLVMFPYPSGDLHM
GHLKNYTMGDVLARFRRMQGYEVLHPMGWDAFGLPAENAALKFGVHPKDW
TYANIRQAKESLRLMGILYDWDREVTTCEPEYYRWNQWIFLKMWEKGLAY
RAKGLVNWCPKCQTVLANEQVVEGRCWRHEDTPVEKRELEQWYLRITAYA
ERLLKDLEGLNWPEKVKAMQRAWIGRSEGAEILFPVEGKEVRIPVFTTRP
DTLFGATFLVLAPEHPLTLELAAPEKREEVLAYVEAAKRKTEIERQAEGR
EKTGVFLGAYALNPATGERIPIWTADYVLFGYGTGAIMAVPAHDQRDYEF
ARKFGLPIKKVIERPGEPLPEPLERAYEEPGIMVNSGPFDGTESEEGKRK
VIAWLEEKGLGKGRVTYRLRDWLISRQRYWGTPIPMVHCEACGVVPVPEE
ELPVLLPDLKDVEDIRPKGKSPLEAHPEFYETTCPKCGGPAKRDTDTMDT
FFDSSWYYLRYTDPHNDRLPFDPEKANAWMPVDQYIGGVEHAVLHLLYSR
FFTKFLHDLGMVKVEEPFQGLFTQGMVLAWTDFGPVEVEGSVVRLPEPTR
IRLEIPESALSLEDVRKMGAELRPHEDGTLHLWKPAVMSKSKGNGVMVGP
FVKEQGADIARITILFAAPPENEMVWTEEGVQGAWRFLNRIYRRVAEDRE
ALLETSGVFQAEALEGKDRELYGKLHETLKKVTEDLEALRFNTAIAALME
FLNALYEYRKDRPVTPVYRTAIRYYLQMLFPFAPHLAEELWHWFWPDSLF
EAGWPELDEKALEKDVVEVAVQVNGRVRGTIHIPKDAPLEVARAEALKVR
NVRAHLEGKEVVKEIYVPGKILNLVV

3D structure

• PDB: 2v0g An Antifungal Agent Inhibits an Aminoacyl-tRNA Synthetase by Trapping tRNA in the Editing Site.
• Chain: D
• Resolution: 3.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F501 H541 F551 V637 K640
• Catalytic site (residue number reindexed from 1): 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	rna	D	V172 E214 K215 S227 F246 T247 T248 R249 K302 Y327 V328 L329 Y332 I337 H343 D344 R346 R418 F666 P669 N672 E679 R686 E750 A820 Q822 V827 N873	V172 E214 K215 S227 F246 T247 T248 R249 K302 Y327 V328 L329 Y332 I337 H343 D344 R346 R418 F666 P669 N672 E679 R686 E750 A820 Q822 V827 N873
BS02	LEU	D	F41 P42 Y43 H541	F41 P42 Y43 H541
BS03	ZN	D	C159 C162	C159 C162

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

External links

• PDB: RCSB:2v0g, PDBe:2v0g, PDBj:2v0g
• PDBsum: 2v0g
• PubMed: 17588934
• UniProt: Q7SIE4