Structure of PDB 8brx Chain A

Receptor sequence
>8brxA (length=544) Species: 562 (Escherichia coli) [Search protein sequence]
AKKILVTCACPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDA
HGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENR
QLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQ
YGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQA
WTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVW
LDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDSTAELYHFIGKDCVYFHSL
FWPAMLEGSNFRKPSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDAD
SLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKR
FDGVLASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANR
YVDEQAPWVVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPKLTERAE
AFLNTELTWDGIQQPLLGHKVNPFKALYNRIDMRQVEALVEASK
3D structure
PDB8brx Redesigning methionyl-tRNA synthetase for beta-methionine activity with adaptive landscape flattening and experiments.
ChainA
Resolution1.54 Å
3D
structure
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Enzymatic activity
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 B3M A A12 C13 D52 P257 Y260 A9 C10 D49 P254 Y257
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:8brx, PDBe:8brx, PDBj:8brx
PDBsum8brx
PubMed37518893
UniProtP00959|SYM_ECOLI Methionine--tRNA ligase (Gene Name=metG)

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