Structure of PDB 3al0 Chain C Binding Site BS01

Receptor Information
>3al0 Chain C (length=564) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KVTKDLVLHLENLARLELSEDQRESLMKDFQEILDYVELLNEVDVEGVEP
MYTPVEDSAKLRKGDPRFFEMRDLIKKNFPEEKDGHIKVPGIPKKIRRCF
ELVRVRFAPSPTGHLHVGGARTALFNWMFARKEGGKFILRIEDTDTERSS
REYEQQILESLRWCGLDWDEGPDIGGDFGPYRQSERLEIYREYAEKLVED
KRAYYVVYDKEDPSKELFTTYEYPHEYKEKGHPVTIKFKVLPGKTSFEDL
LKGYMEFDNSTLEDFIIMKSNGFPTYNFAVVVDDHLMRISHVFRGEDHLS
NTPKQLMIYEAFGWEAPVFMHIPLILGSDRTPLSKRHGATSVEHFRREGI
LSRALMNYLALLGWRVEGDEIFTIEEKLQSFDPKDISNKGVIFDYQKLEW
VNGKHMRRIDLEDLKREFIEWAKYAGKEIPSVDERYFSETLRICREKVNT
LSQLYDIMYPFMNDDYEYEKDYVEKFLKREEAERVLEEAKKAFKDLNSWN
MEEIEKTLRDLSEKGLASKKVVFQLIRGAVTGKLVTPGLFETIEVLGKER
TLKRLERTLQFLKK
Ligand information
>3al0 Chain E (length=74) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ugggaggucgucuaacgguaggacggcggacucuggauccgcugguggag
guucgaguccuccccucccagcca
<<<<<<<..<<<<.......>>>><<<<<<.......>>>>>>...<<<<
<.......>>>>>>>>>>>>....
Receptor-Ligand Complex Structure
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PDB3al0 Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions.
Resolution3.368 Å
Binding residue
(original residue number in PDB)		T170 D171 R174 Y234 P239 K278 M281 I292 K295 S296 Y302 D323 H324 L325 S326 N327 K330 R356 P358 G389 W390 R391 E396 S413 K415 V417 I418 K423 W426 R433 E472 K473 Q479 I483 R535 K546 Q550 R553 V561 T562 G564 L565
Binding residue
(residue number reindexed from 1)		T144 D145 R148 Y208 P213 K252 M255 I266 K269 S270 Y276 D297 H298 L299 S300 N301 K304 R330 P332 G363 W364 R365 E370 S387 K389 V391 I392 K397 W400 R407 E446 K447 Q453 I457 R509 K520 Q524 R527 V535 T536 G538 L539
Enzymatic activity
Catalytic site (original residue number in PDB) S136 K361
Catalytic site (residue number reindexed from 1) S110 K335
Enzyme Commision number 6.1.1.17: glutamate--tRNA ligase.
6.3.5.-
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004818 glutamate-tRNA ligase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016874 ligase activity
GO:0050566 asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity
GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006424 glutamyl-tRNA aminoacylation
GO:0006450 regulation of translational fidelity
GO:0043039 tRNA aminoacylation
GO:0070681 glutaminyl-tRNAGln biosynthesis via transamidation
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:3al0, PDBe:3al0, PDBj:3al0
PDBsum3al0
PubMed20882017
UniProtQ9WY94;
Q9X2I8|SYE2_THEMA Glutamate--tRNA ligase 2 (Gene Name=gltX2)

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