Structure of PDB 2yy5 Chain C

Receptor sequence
>2yy5C (length=336) Species: 272634 (Mycoplasmoides pneumoniae M129) [Search protein sequence]
MKRALTGIQASGKQHLGNYLGVMQSLIELQEQCQLFVFVADLHSITVDFQ
PQALKQNNFDLVRTLLAVGLDPQKACLFLQSDLLEHSMMGYLMMVQSNLG
ELQRMTQFKAKKALNIPTGLLTYPALMAGDILLYQPDIVPVGNDQKQHLE
LTRDLAQRIQKKFKLKLRLPQFVQNKDTNRIMDLFDPTKKMSKSSKNQNG
VIYLDDPKEVVVKKIRQATTDSFNKIRFASKTQPGVTNMLTILKALLKEP
VNQSLTNQLGNDLEAYFSTKSYLDLKNALTEATVNLLVNIQRKREQISRE
QVFNCLQAGKNQAQATARTTLALFYDGFGLGSQNIK
3D structure
PDB2yy5 Crystal Structure of tryptophanyl-tRNA synthetase from Mycoplasma pneumoniae
ChainC
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K112 K200 K203
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 WSA C G8 Q10 G18 N19 G22 F39 H44 M137 I141 V151 G152 D154 Q155 N189 R190 I191 G7 Q9 G17 N18 G21 F38 H43 M127 I131 V141 G142 D144 Q145 N179 R180 I181
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:2yy5, PDBe:2yy5, PDBj:2yy5
PDBsum2yy5
PubMed
UniProtP75510|SYW_MYCPN Tryptophan--tRNA ligase (Gene Name=trpS)

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