Structure of PDB 3sz3 Chain A

Receptor sequence
>3sz3A (length=341) Species: 243277 (Vibrio cholerae O1 biovar El Tor str. N16961) [Search protein sequence]
SNAMSKPIVLSGVQPSGELSIGNYLGALRQWQQMQDDYDCQYCVVDLHAI
TVRQDPQALHEATLDALAICLAVGVDPKKSTLFVQSHVPEHAQLGWVLNC
YTQMGELSRMTQFKDKSARYANDVNAGLFGYPVLMAADILLYGAHQVPVG
SDQKQHLELARDIATRFNNIYSPEQPIFTIPEPYIPTVNARVMSLQDATK
KMSKSDDNRKNVITLLEDPKSIIKKINKAQTDAETPPRIAYDVENKAGIA
NLMGLYSAATGKTFAEIEAQYAGVEMYGPFKKDVGEAVVAMLEPVQAEYQ
RIRNDREYLNSVMRDGAEKASAKALQTLKKVYAAVGFVARP
3D structure
PDB3sz3 Crystal structure of Tryptophanyl-tRNA synthetase from Vibrio cholerae with an endogenous tryptophan
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K113 K198 K201
Catalytic site (residue number reindexed from 1) K116 K201 K204
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 L7 G9 Q11 V42 H45 M132 D135 V144 Q150 L10 G12 Q14 V45 H48 M135 D138 V147 Q153
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
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3sz3, PDBe:3sz3, PDBj:3sz3
PDBsum3sz3
PubMed
UniProtQ9KNV7|SYW_VIBCH Tryptophan--tRNA ligase (Gene Name=trpS)

[Back to BioLiP]