Structure of PDB 1f4l Chain A

Receptor sequence
>1f4lA (length=545) Species: 562 (Escherichia coli) [Search protein sequence]
AKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDA
HGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENR
QLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQ
YGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQA
WTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVW
LDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSL
FWPAMLEGSNFRKPSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDAD
SLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKR
FDGVLASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANR
YVDEQAPWVVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPKLTERAE
AFLNTELTWDGIQQPLLGHKVNPFKALYNRIDMRQVEALVEASKE
3D structure
PDB1f4l How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L13 H21 H24 D52 D129 K132 S175 S178 K332 K335
Catalytic site (residue number reindexed from 1) L10 H18 H21 D49 D126 K129 S172 S175 K329 K332
Enzyme Commision number 6.1.1.10: methionine--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 ZN A C145 C148 C158 C161 C142 C145 C155 C158
BS02 MET A L13 Y15 D52 W253 A256 P257 Y260 H301 L10 Y12 D49 W250 A253 P254 Y257 H298
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004825 methionine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006431 methionyl-tRNA aminoacylation

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Molecular Function
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Biological Process
External links
PDB RCSB:1f4l, PDBe:1f4l, PDBj:1f4l
PDBsum1f4l
PubMed11243794
UniProtP00959|SYM_ECOLI Methionine--tRNA ligase (Gene Name=metG)

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