Structure of PDB 5mgh Chain A

Receptor sequence
>5mghA (length=405) Species: 9606 (Homo sapiens) [Search protein sequence]
PGSVVELLGKSYPQDDHSNLTRKVLTRVGRNLHNQQHHALWLIKERVKEH
FYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYL
NRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRRDQIDSQHYPIFHQLEA
VRLFSKHELFAGIKDGESLQLFEQSSRSAHKQETHTMEAVKLVEFDLKQT
LTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQ
QLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQFCVS
NINQKVKFQPLSKYPAVINDISFWLPSENYAENDFYDLVRTIGGDLVEKV
DLIDKFVHPKTHKTSHCYRITYRHMERTLSQREVRHIHQALQEAAVQLLG
VEGRF
3D structure
PDB5mgh Kinetic and structural changes in HsmtPheRS, induced by pathogenic mutations in human FARS2.
ChainA
Resolution1.87 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) G95 H109 R133 Q147 T225 A265
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 H109 S111 E149 F222 F224 G244 C245 F266 G267
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:5mgh, PDBe:5mgh, PDBj:5mgh
PDBsum5mgh
PubMed28419689
UniProtO95363|SYFM_HUMAN Phenylalanine--tRNA ligase, mitochondrial (Gene Name=FARS2)

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