Structure of PDB 3tzl Chain B

Receptor sequence
>3tzlB (length=320) Species: 192222 (Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819) [Search protein sequence]
AMRVLTGLQPSGDLHIGNYFGAIKQMVDAQEKSQMFMFIANYHAMTSSQD
GEKLKQNSLKAAAAFLSLGIDPQKSVFWLQSDVKEVMELYWILSQFTPMG
LLERAHSYKDKVAKGLSASHGLFSYPVLMAADILLFDTRIVPVGKDQIQH
VEIARDIALKVNNEWGEIFTLPEARVNEEVAVVVGTDGAKMSKSYQNTID
IFSSEKTLKKQISSIVTDSTALEDPKDHENCNIFKIAKLFLDESGQKELQ
IRYEKGGEGYGHFKIYLNELVNAYFKEAREKYNELLEKPSHLKEILDFGA
TKARKIAQEKMQKIYEKIGL
3D structure
PDB3tzl Crystal Structure of Tryptophanyl-tRNA Synthetase from Campylobacter jejuni complexed with ADP and Tryptophane
ChainB
Resolution2.154 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K110 K189 K192
Catalytic site (residue number reindexed from 1) K111 K190 K193
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 ADP B H14 G16 N17 G20 V182 M190 S191 K192 H15 G17 N18 G21 V183 M191 S192 K193
BS02 TRP B G6 F37 H42 M128 I132 V140 Q146 G7 F38 H43 M129 I133 V141 Q147
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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Biological Process
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Cellular Component
External links
PDB RCSB:3tzl, PDBe:3tzl, PDBj:3tzl
PDBsum3tzl
PubMed
UniProtQ9PIB4|SYW_CAMJE Tryptophan--tRNA ligase (Gene Name=trpS)

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