Structure of PDB 4q2x Chain B

Receptor sequence
>4q2xB (length=582) Species: 9606 (Homo sapiens) [Search protein sequence]
ASMINIISRLQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDYQCNSAMG
ISQMLKKEQKVNPREIAENITKHLPDNECIEKVEIAGPGFINVHLRKDFV
SEQLTSLLVNGVQLPALNKKVIVDFSSPNIAKEMHVGHLRSTIIGESISR
LFEFAGYDVLRLNHVGDWGTQFGMLIAHLQDKFPDYLTVSPPIGDLQVFY
KESKKRFDTEEEFKKRAYQCVVLLQGKNPDITKAWKLICDVSRQELNKIY
DALDVSLIERGESFYQDRMNDIVKEFEDRGFVQVDDGRKIVFVPGCSIPL
TIVKSDGGYTYDTSDLAAIKQRLFEEKADMIIYVVDNGQSVHFQTIFAAA
QMIGWYDPKVTRVFHAGFGVVLGEDKKKFKTRETVRLMDLLGEGLKRSMD
KLKEKERDKVLTAEELNAAQTSVAYGCIKYADLSRNRLNDYIFSFDKMLD
DRGNTAAYLLYAFTRIRSIARLANIDEEMLQKAARETKILLDHEKEWKLG
RCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYDSCYCVDRQTGKL
KVNMWRMLLCEAVAAVMAKGFDILGIKPVQRM
3D structure
PDB4q2x The crystal structure of arginyl-tRNA synthetase from Homo sapiens
ChainB
Resolution2.798 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K133 H136 H139
Catalytic site (residue number reindexed from 1) K132 H135 H138
Enzyme Commision number 6.1.1.19: arginine--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 GGB B D125 S128 N130 H165 Y312 D316 Y334 V336 D124 S127 N129 H164 Y311 D315 Y333 V335
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004814 arginine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006420 arginyl-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:4q2x, PDBe:4q2x, PDBj:4q2x
PDBsum4q2x
PubMed24859084
UniProtP54136|SYRC_HUMAN Arginine--tRNA ligase, cytoplasmic (Gene Name=RARS1)

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