Structure of PDB 1obh Chain A

Receptor sequence
>1obhA (length=762) Species: 262724 (Thermus thermophilus HB27) [Search protein sequence]
MEKYNPHAIEAKWQRFWEEKGFMKAKDLPGGGKQYVLVMFPYPSGDLHMG
HLKNYTMGDVLARFRRMQGYEVLHPMGWDAFGLPAENAALKFGVHPKDWT
YANIRQAKESLRLMGILYDWDREVTTCEPEYYRWNQWIFLKMWEKGLAYR
AKEQWYLRITAYAERLLKDLEGLNWPEKVKAMQRAWIGRSEGAEILFPVE
GKEVRIPVFTTRPDTLFGATFLVLAPEHPLTLELAAPEKREEVLAYVEAA
KRKTEIERQAEGREKTGVFLGAYALNPATGERIPIWTADYVLFGYGTGAI
MAVPAHDQRDYEFARKFGLPIKKVIERPGEPLPEPLERAYEEPGIMVNSG
PFDGTESEEGKRKVIAWLEEKGLGKGRVTYRLRDWLISRQRYWGTPIPMV
HCVVPVPEEELPVLLPDLKDVEDISPLEAHPEFYETTCPKRDTDTMDTFF
DSSWYYLRYTDPHNDRLPFDPEKANAWMPVDQYIGGVEHAVLHLLYSRFF
TKFLHDLGMVKVEEPFQGLFTQGMVLAWTDFGPVEVEGSVVRLPEPTRIR
LEIPESALSLEDVRKMGAELRPHEDGTLHLWKPAVMSKSKGNGVMVGPFV
KEQGADIARITILFAAPPENEMVWTEEGVQGAWRFLNRIYRRVAEDREAL
LETSGVFQAEALEGKDRELYGKLHETLKKVTEDLEALRFNTAIAALMEFL
NALYEYRKDRPVTPVYRTAIRYYLQMLFPFAPHLAEELWHWFWPDSLFEA
GWPELDEKALEK
3D structure
PDB1obh Structural and Mechanistic Basis of Pre- and Posttransfer Editing by Leucyl-tRNA Synthetase
ChainA
Resolution2.2 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 F501 H541 F551 V637 K640
Catalytic site (residue number reindexed from 1) F40 H48 H51 D79 F449 H489 F499 V585 K588
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 NVA A F41 Y43 D80 H545 F40 Y42 D79 H493
BS02 LMS A P42 Y43 G51 N55 M576 V577 P41 Y42 G50 N54 M524 V525
BS03 NVA A M338 V340 D347 M301 V303 D310
BS04 LMS A T247 T248 V328 L329 Y332 I337 D344 T210 T211 V291 L292 Y295 I300 D307
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:1obh, PDBe:1obh, PDBj:1obh
PDBsum1obh
PubMed12718881
UniProtQ72GM3

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