Structure of PDB 1ady Chain A

Receptor sequence
>1adyA (length=420) Species: 274 (Thermus thermophilus) [Search protein sequence]
TARAVRGTKDLFGKELRMHQRIVATARKVLEAAGALELVTPIFEETQVFE
KGVGAATDIVRKEMFTFQDRGGRSLTLRPEGTAAMVRAYLEHGMKVWPQP
VRLWMAGPMFRAERPQKGRYRQFHQVNYEALGSENPILDAEAVVLLYECL
KELGLRRLKVKLSSVGDPEDRARYNAYLREVLSPHREALSEDSKERLEEN
PMRILDSKSERDQALLKELGVRPMLDFLGEEARAHLKEVERHLERLSVPY
ELEPALVRGLDYYVRTAFEVHHEEIGAQSALGGGGRYDGLSELLGGPRVP
GVGFAFGVERVALALEAEGFGLPEEKGPDLYLIPLTEEAVAEAFYLAEAL
RPRLRAEYALAPRKPAKGLEEALKRGAAFAGFLGEDELRAGEVTLKRLAT
GEQVRLSREEVPGYLLQALG
3D structure
PDB1ady Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase.
ChainA
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.21: histidine--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 HAM A E81 T83 R112 E114 G119 Y121 F124 E130 R259 Y263 Y264 A281 L282 G283 Y288 G304 F305 A306 G308 R311 E80 T82 R111 E113 G118 Y120 F123 E129 R258 Y262 Y263 A280 L281 G282 Y287 G303 F304 A305 G307 R310
Gene Ontology
Molecular Function
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004821 histidine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006412 translation
GO:0006427 histidyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1ady, PDBe:1ady, PDBj:1ady
PDBsum1ady
PubMed9115984
UniProtP56194|SYH_THET8 Histidine--tRNA ligase (Gene Name=hisS)

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