Structure of PDB 5mgw Chain A

Receptor sequence
>5mgwA (length=406) Species: 9606 (Homo sapiens) [Search protein sequence]
APGSVVELLGKSYPQDDHSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKE
HFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYY
LNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRRDQIDSQHYPIFHQLE
AVRLFSKHELFAGIKDGESLQLFEQSSRSAHKQETHTMEAVKLVEFDLKQ
TLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVME
QQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQFCV
SNINQKVKFQPLSKYPAVINDISFWLPSENYAENDFYDLVRTIGGDLVEK
VDLIDKFVHPKTHKTSHCYRITYCHMERTLSQREVRHIHQALQEAAVQLL
GVEGRF
3D structure
PDB5mgw Kinetic and structural changes in HsmtPheRS, induced by pathogenic mutations in human FARS2.
ChainA
Resolution1.46 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) G96 H110 R134 Q148 T226 A266
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 A275 F276 G277 H110 S112 E150 F223 F225 G245 C246 A266 F267 G268
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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Cellular Component
External links
PDB RCSB:5mgw, PDBe:5mgw, PDBj:5mgw
PDBsum5mgw
PubMed28419689
UniProtO95363|SYFM_HUMAN Phenylalanine--tRNA ligase, mitochondrial (Gene Name=FARS2)

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