Structure of PDB 4eg5 Chain A

Receptor sequence
>4eg5A (length=521) [Search protein sequence]
EKVFFVTSPIYYVNAAPHIGHVYSTLITDVIGRYHRVKGERVFALTGTDE
HGQKVAEAAKQKQVSPYDFTTAVAGEFKKCFEQMDYSIDYFIRTTNEQHK
AVVKELWTKLEQKGDIYLGRYEGWYSISDESFLTPQNITDGVDKDGNPCK
VSLESGHVVTWVSEENYMFRLSAFRERLLEWYHANPGCIVPEFRRREVIR
AVEKGLPDLSVSRARATLHNWAIPVPGNPDHCVYVWLDALTNYLTGSRLR
VDESGKEVSLVDDFNELERFPADVHVIGKDILKFHAIYWPAFLLSAGLPL
PKKIVAHGWWTKDRKVFDPVEKAEEFGYDALKYFLLRESGFSDDGDYSDK
NMIARLNGELADTLGNLVMRCTSAKINVNGEWPSPAAYTEEDESLIQLIK
DLPGTADHYYLIPDIQKAIIAVFDVLRAINAYVTDMAPWKLVKTDPERLR
TVLYITLEGVRVTTLLLSPILPRKSVVIFDMLGVPEVHRKGIENFEFGAV
PPGTRLGPAVEGEVLFSKRST
3D structure
PDB4eg5 Distinct States of Methionyl-tRNA Synthetase Indicate Inhibitor Binding by Conformational Selection.
ChainA
Resolution3.1 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
Catalytic site (residue number reindexed from 1) H18 H21 S126 D129 S152 S155
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 A P247 I248 Y250 D287 W474 Y481 H523 K550 P9 I10 Y12 D49 W236 Y243 H285 K312
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:4eg5, PDBe:4eg5, PDBj:4eg5
PDBsum4eg5
PubMed22902861
UniProtQ38C91

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