Structure of PDB 3a05 Chain A

Receptor sequence
>3a05A (length=367) Species: 56636 (Aeropyrum pernix) [Search protein sequence]
LDPWGAVEIKDYDRLLRTFGIRPFSEVLPLLRKAGMEPSFLMRRGIIFGH
RDFDKILEAKARGERVAVLTGFMPSGKFHFGHKLTVDQLIYLQKNGFKVF
VAIADAEAFAVRRIGREEAVRIAVEEYIANMIALGLDPKDTEFYFQTNRG
TPYFRLIQLFSGKVTAAEMEAIYGELTPAKMMASLTQAADILHVQLDEYG
GYRHVVVPVGADQDPHLRLTRDLADRMAGVVELERPASTYHKLQPGLDGR
KMSSSRPDSTIFLTDPPEVARNKLFRALTGGRATAEEQRRLGGVPEVCSV
YHMDLYHLMPDDGEVKHIYTSCRLGKILCGECKQIAWEKLERFLAEHQSR
LEKAKTIAWKLVEPPRF
3D structure
PDB3a05 Molecular Recognition of Tryptophan tRNA by Tryptophanyl-tRNA Synthetase from Aeropyrum pernix K1
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) K185 G254 M257
Catalytic site (residue number reindexed from 1) K180 G249 M252
Enzyme Commision number 6.1.1.2: tryptophan--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 TRP A G76 Q192 D195 G71 Q187 D190
BS02 SF4 A T284 G285 G286 C303 V305 C327 C334 C337 T279 G280 G281 C298 V300 C322 C329 C332
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004830 tryptophan-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006436 tryptophanyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:3a05, PDBe:3a05, PDBj:3a05
PDBsum3a05
PubMed
UniProtQ9Y924|SYW_AERPE Tryptophan--tRNA ligase (Gene Name=trpS)

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