Structure of PDB 1htt Chain B

Receptor sequence
>1httB (length=357) Species: 562 (Escherichia coli) [Search protein sequence]
NIQAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFK
RAIGEVTDVVEKEMYTFEDRNGDSLTLRPEGTAGCVRAGIEHGLLYNQEQ
RLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWR
ALGISEHVTLELNSIGDEESREHFAGLCKLLESAGIAYTVNQRLVRGLDY
YNRTVFEWVTNQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQ
AVNPEFKADPVVDIYLVASGADTQSAAMALAERLRDELPGVKLMTNHGGG
NFKKQFARADKWGARVAVVLGESEVANGTAVVKDLRSGEQTAVAQDSVAA
HLRTLLG
3D structure
PDB1htt Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate.
ChainB
Resolution2.6 Å
3D
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
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 HIS B T85 E131 L261 Y263 Y264 Y288 G304 F305 T82 E128 L198 Y200 Y201 Y221 G237 F238
BS02 AMP B R113 E115 G120 R121 Y122 F125 Q127 R259 T281 G308 R311 R110 E112 G117 R118 Y119 F122 Q124 R196 T214 G241 R244
Gene Ontology
Molecular Function
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004821 histidine-tRNA ligase activity
GO:0005524 ATP binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006412 translation
GO:0006427 histidyl-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:1htt, PDBe:1htt, PDBj:1htt
PDBsum1htt
PubMed7556055
UniProtP60906|SYH_ECOLI Histidine--tRNA ligase (Gene Name=hisS)

[Back to BioLiP]