Structure of PDB 1pg2 Chain A

Receptor sequence
>1pg2A (length=488) Species: 562 (Escherichia coli) [Search protein sequence]
AKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDA
HGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENR
QLSELIYSRLKENGFIKNRTISRDSEHFFFDLPSFSEMLQAWTRSGALQE
QVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVWLDAPIGYMG
SFKNLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGS
NFRKPSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAK
LSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLASEL
ADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWV
VAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPKLTERAEAFLNTELTW
DGIQQPLLGHKVNPFKALYNRIDMRQVEALVEASKEEV
3D structure
PDB1pg2 Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase.
ChainA
Resolution1.75 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 K332 K335
Catalytic site (residue number reindexed from 1) L10 H18 H21 D49 K270 K273
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 ADN A A12 G23 H24 E27 G294 D296 Y325 V326 A9 G20 H21 E24 G232 D234 Y263 V264
BS02 MET A A12 L13 Y15 D52 W253 A256 P257 Y260 A9 L10 Y12 D49 W191 A194 P195 Y198 PDBbind-CN: -logKd/Ki=4.96,Kd=11uM
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:1pg2, PDBe:1pg2, PDBj:1pg2
PDBsum1pg2
PubMed12946347
UniProtP00959|SYM_ECOLI Methionine--tRNA ligase (Gene Name=metG)

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