Structure of PDB 4py2 Chain A

Receptor sequence
>4py2A (length=495) Species: 359391 (Brucella abortus 2308) [Search protein sequence]
REKYYITTAIAYPNGKPHIGHAYELIATDAMARFQRLNGMDVYFLTGTDE
HGIKMLQSARKEGITPRDLADRNTSAFRRMAEVLNSSNDDYIRTSEERHY
KASQAIWQAMVANGDIYKGGYAGWYSVRDEAYYGEEETEVRADGVRYGPQ
GTPVEWVEEESYFFRLSAYQDKLLDLYENNPGFIMPAERRNEIVSFVKSG
LKDLSISRTTFDWGIPVPGDEKHVMYVWVDALTNYITALGYPDTTDERWA
YWPANAHIIGKDISRFHAVYWPAFLMSAQLPLPKRVFAHGFLFNRIDPFE
LVERYGLDQLRYFLMREVPFGQDGSYSHEAIVNRTNADLANDLGNLAQRS
LSMIAKNCEGKVPQPGAFSEADKAILDQADAALETARKAMDDQALHLALG
AIFAVVAEANRYFAGQEPWALRKTDPARMGTVLYVTAEVLRRVGIMVQPF
IPQSAEKLLDILAVPADKRQFADVLASPLAGGTDLPAPQPVFPRY
3D structure
PDB4py2 Brucella melitensis Methionyl-tRNA-Synthetase (MetRS), a Potential Drug Target for Brucellosis.
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I12 H20 H23 D51 S128 D131 G150 W230 I265
Catalytic site (residue number reindexed from 1) I10 H18 H21 D49 S126 D129 G148 W228 I263
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 43E A A11 I12 Y14 D51 H53 G54 M227 Y228 V229 W230 D232 I265 F268 H269 A9 I10 Y12 D49 H51 G52 M225 Y226 V227 W228 D230 I263 F266 H267 MOAD: ic50=0.272uM
PDBbind-CN: -logKd/Ki=6.57,IC50=0.272uM
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:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006431 methionyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:4py2, PDBe:4py2, PDBj:4py2
PDBsum4py2
PubMed27500735
UniProtQ2YQ76

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