Structure of PDB 4eg1 Chain B

Receptor sequence
>4eg1B (length=533) [Search protein sequence]
GPGSMKVEKVFFVTSPIYYVNAAPHIGHVYSTLITDVIGRYHRVKGERVF
ALTGTDEHGQKVAEAAKQKQVSPYDFTTAVAGEFKKCFEQMDYSIDYFIR
TTNEQHKAVVKELWTKLEQKGDIYLGRYEGWYSISDESFLTPQNITDGVD
PCKVSLESGHVVTWVSEENYMFRLSAFRERLLEWYHANPGCIVPEFRRRE
VIRAVEKGLPDLSVSRARATLHNWAIPVPGNPDHCVYVWLDALTNYLTGS
RLRVDESGKEVSLVDDFNELERFPADVHVIGKDILKFHAIYWPAFLLSAG
LPLPKKIVAHGWWTKDRKKISKSLGNVFDPVEKAEEFGYDALKYFLLRES
GFSDDGDYSDKNMIARLNGELADTLGNLVMRCTSAKINVNGEWPSPAAYT
EEDESLIQLIKDLPGTADHYYLIPDIQKAIIAVFDVLRAINAYVTDMAPW
KLVKTDPERLRTVLYITLEGVRVTTLLLSPILPRKSVVIFDMLGVPEVHR
KGIENFEFGAVPPGTRLGPAVEGEVLFSKRSTE
3D structure
PDB4eg1 Distinct States of Methionyl-tRNA Synthetase Indicate Inhibitor Binding by Conformational Selection.
ChainB
Resolution2.9 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 S155 S158 K319 K322
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 MET B I248 Y250 D287 W474 A477 L478 Y481 H523 I17 Y19 D56 W239 A242 L243 Y246 H288
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:4eg1, PDBe:4eg1, PDBj:4eg1
PDBsum4eg1
PubMed22902861
UniProtQ38C91

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