Structure of PDB 4ega Chain B

Receptor sequence
>4egaB (length=528) [Search protein sequence]
GPGSMKVEKVFFVTSPIYYVNAAPHIGHVYSTLITDVIGRYHRVKGERVF
ALTGTDEHGQKVAEAAKQKQVSPYDFTTAVAGEFKKCFEQMDYSIDYFIR
TTNEQHKAVVKELWTKLEQKGDIYLGRYEGWYSISDESFLTPQNITDCKV
SLESGHVVTWVSEENYMFRLSAFRERLLEWYHANPGCIVPEFRRREVIRA
VEKGLPDLSVSRARATLHNWAIPVPGNPDHCVYVWLDALTNYLTGSRLRV
DESGKEVSLVDDFNELERFPADVHVIGKDILKFHAIYWPAFLLSAGLPLP
KKIVAHGWWTKDRKKISKSLGNVFDPVEKAEEFGYDALKYFLLRESGFSD
DGDYSDKNMIARLNGELADTLGNLVMRCTSAKINVNGEWPSPAAYTEEDE
SLIQLIKDLPGTADHYYLIPDIQKAIIAVFDVLRAINAYVTDMAPWKLVK
TDPERLRTVLYITLEGVRVTTLLLSPILPRKSVVIFDMLGVPEVHRKGIE
NFEFGAVPPGTRLGPAVEGEVLFSKRST
3D structure
PDB4ega Distinct States of Methionyl-tRNA Synthetase Indicate Inhibitor Binding by Conformational Selection.
ChainB
Resolution2.698 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H256 H259 S364 D367 S390 S393 K554 K557
Catalytic site (residue number reindexed from 1) H25 H28 S133 D136 S151 S154 K315 K318
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 0P8 B P247 I248 Y250 D287 H289 G290 Y472 V473 W474 D476 L478 F522 H523 P16 I17 Y19 D56 H58 G59 Y233 V234 W235 D237 L239 F283 H284
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:4ega, PDBe:4ega, PDBj:4ega
PDBsum4ega
PubMed22902861
UniProtQ38C91

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