Structure of PDB 4eg4 Chain B

Receptor sequence
>4eg4B (length=511) [Search protein sequence]
GPGSMKVEKVFFVTSPIYYVNAAPHIGHVYSTLITDVIGRYHRVKGERVF
ALTGTDEHGQKVAEAAKQKQVSPYDFTTAVAGEFKKCFEQMDYSIDYFIR
TTNEQHKAVVKELWTKLEQKGDIYLGRYEGWYSISDESFLTPQNITWVSE
ENYMFRLSAFRERLLEWYHANPGCIVPEFRRREVIRAVEKGLPDLSVSRA
RATLHNWAIPVPGNPDHCVYVWLDALTNYLTGSRLRVDESGKEVSLVDDF
NELERFPADVHVIGKDILKFHAIYWPAFLLSAGLPLPKKIVAHGWWTKDR
KKISLGNVFDPVEKAEEFGYDALKYFLLRESGDDGDYSDKNMIARLNGEL
ADTLGNLVMRCTSAKINVNGEWPSPAAYTEEDESLIQLIKDLPGTADHYY
LIPDIQKAIIAVFDVLRAINAYVTDMAPWKLVKTDPERLRTVLYITLEGV
RVTTLLLSPILPRKSVVIFDMLGVPEVHRKGIENFEFGAVPPGTRLGPAV
EGEVLFSKRST
3D structure
PDB4eg4 Distinct States of Methionyl-tRNA Synthetase Indicate Inhibitor Binding by Conformational Selection.
ChainB
Resolution3.151 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 K554
Catalytic site (residue number reindexed from 1) H25 H28 S133 D136 K302
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 0OT B P247 I248 Y250 D287 H289 G290 Y472 V473 W474 D476 I519 H523 P16 I17 Y19 D56 H58 G59 Y220 V221 W222 D224 I267 H271
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:4eg4, PDBe:4eg4, PDBj:4eg4
PDBsum4eg4
PubMed22902861
UniProtQ38C91

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