Structure of PDB 5e3i Chain A

Receptor sequence
>5e3iA (length=388) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
SSIVAIKGFNDVLPTQTAAWRRLEQHLASLMDAYGYQQIRLPIVEQTGLF
KRAIGDATDIVEKEMYTFFDKGNPPESLTLRPEGTAGCVRALVEHNLLRG
ATPRVWYMGPMFRYEKPQKGRYRQFHQFGVETFGVATPDIDAELIMLTAR
LWKRMGVDHMVQLELNTLGETDERTEYRNAAPKLHDFLKEDSLSHFQQLQ
DYLTAAGIKFVINQKLVRGLDYYNKTVFEWTTTALGSQGTVCAGGRYDGL
VGQLKGKADQSVPAVGFAMGMERLLLLLEQVEQAEIVRDCEAFLVAEPAY
QSKALVLAEQLRDQLEAANSNIRIKTGSQGSMKSQMKKADQAGAVYAIIL
GEREWEAQQLAVKELATAEQSQVALAELVPFLIEKFTK
3D structure
PDB5e3i Crystal Structure of a Histidyl-tRNA synthetase from Acinetobacter baumannii with bound L-Histidine and ATP
ChainA
Resolution2.2 Å
3D
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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 ATP A R115 E117 G122 R123 Y124 F127 Q129 R261 T283 V284 G313 R316 R113 E115 G120 R121 Y122 F125 Q127 R218 T240 V241 G270 R273
BS02 HIS A E85 T87 E133 Y265 Y266 Y290 G309 F310 A311 E83 T85 E131 Y222 Y223 Y247 G266 F267 A268
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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Cellular Component
External links
PDB RCSB:5e3i, PDBe:5e3i, PDBj:5e3i
PDBsum5e3i
PubMed
UniProtB0VKR7|SYH_ACIBS Histidine--tRNA ligase (Gene Name=hisS)

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