Structure of PDB 5mgu Chain A

Receptor sequence
>5mguA (length=407) Species: 9606 (Homo sapiens) [Search protein sequence]
AAPGSVVELLGKSYPQDDHSNLTRKVLTRVGRNLHNQQHHPLWLIKERVK
EHFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNY
YLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRRDQIDSQHYPIFHQL
EAVRLFSKHELFAGIKDGESLQLFEQSSRSAHKQETHTMEAVKLVEFDLK
QMLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVM
EQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQFC
VSNINQKVKFQPLSKYPAVINDISFWLPSENYAENDFYDLVRTIGGDLVE
KVDLIDKFVHPKTHKTSHCYRITYRHMERTLSQREVRHIHQALQEAAVQL
LGVEGRF
3D structure
PDB5mgu Kinetic and structural changes in HsmtPheRS, induced by pathogenic mutations in human FARS2.
ChainA
Resolution1.89 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G105 H119 R143 Q157 T235 A275
Catalytic site (residue number reindexed from 1) G97 H111 R135 Q149 T227 A267
Enzyme Commision number 6.1.1.20: phenylalanine--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 PHE A H119 S121 E159 F232 F234 G254 C255 F276 G277 H111 S113 E151 F224 F226 G246 C247 F268 G269
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004826 phenylalanine-tRNA ligase activity
GO:0005515 protein binding
GO:0005524 ATP binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006432 phenylalanyl-tRNA aminoacylation
GO:0008033 tRNA processing
GO:0043039 tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5mgu, PDBe:5mgu, PDBj:5mgu
PDBsum5mgu
PubMed28419689
UniProtO95363|SYFM_HUMAN Phenylalanine--tRNA ligase, mitochondrial (Gene Name=FARS2)

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