Structure of PDB 3ial Chain A

Receptor sequence
>3ialA (length=496) Species: 184922 (Giardia lamblia ATCC 50803) [Search protein sequence]
TFSLTKTRDTFADWFDAIMDAAELVDRRYPVKGCVVFRPYGFFMENAIMR
LCEEEYAKVGISQILFPTVIPESFLKKESDHIKGFEAECFWVEKGGLQPL
EERLALRPTSETAIYSMFSKWVRSYKDLPLKIHQTCTIFRHETKNTKPLI
RVREIHWNEAHCCHATAEDAVSQLSDYWKVIDTIFSDELCFKGQKLRRVC
WDRFPGADYSEVSDVVMPCGRVLQTAGIHNLGQRFSSTFDILYANKANES
VHPYLTCAGISTRVLACALSIHGDSGGLVLPPLIAPIHVVIIPIGCGKKN
NQESDQQVLGKVNEIADTLKSKLGLRVSIDDDFSKSMGDKLYYYELKGVP
LRIEVGQRDLANGQCIVVPRDVGKDQKRVIPITEVMKVSVVKNVIKDELD
AYKARLKEKAFAFHNSMVTNCKSFDEIVACIENKGGLARFPFYTTEADGE
VWDKKLKDACSAEIRGHNPDENVLPGEVCALSGKPAVCYMYCAKSY
3D structure
PDB3ial Structure of the prolyl-tRNA synthetase from the eukaryotic pathogen Giardia lamblia.
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.15: proline--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 PR8 A T146 E148 I187 V189 I192 W194 E196 F241 Q261 H266 C294 A295 G296 S298 R300 T109 E111 I150 V152 I155 W157 E159 F204 Q224 H229 C257 A258 G259 S261 R263
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004827 proline-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006433 prolyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ial, PDBe:3ial, PDBj:3ial
PDBsum3ial
PubMed22948920
UniProtA8BR89

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