Structure of PDB 5urb Chain B

Receptor sequence
>5urbB (length=546) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
MRKILVTNALPYANGPIHMGHLLGYIQADIWVRAMRAMGHDVTYVCADDA
HGTAIMLRAEANGISPEEQIANVQKEHIRDFDGFGVHFDHYDSTHSDANK
ARSTDIYIKNREAGNIAVRPVTQLFDPEKGMFLSDRFIKGTCPKCKSEDQ
YGDSCEVCGTTYNATELLNPRSTLSGATPVEKSSDHYFFKLPNFAEYLQK
WTRDEGRLPLSIANKLDEWFEAGLADWDISRDAPYFGFEIPDAPNKYFYV
WVDAPIGYMSSFENYIKTKRPDLNFDDFWKKDSQNEVYHFIGKDIVYFHA
LFWPAMLEGANYRTPTGLFVNGFLTVNGQKMSKSRGTFIKAETYLQHLNP
EYLRYYFASKLSDKVEDSDLNLDDFVQKVNSDLVGKVVNIASRCAKFINS
SFNNTLSSTCAESDLVQSFIDAGDSIAAAYEAREFSTAIREIMALADRAN
QYIDEKKPWALAKQEGQEQQVLDVCSVGINLFRQLAVYLAPVLPTLAQQV
QDFLKLESFDFESRKQILVSHEIAQFQPLMQRVDPKAVAAMVDASK
3D structure
PDB5urb Crystal Structure of Methionyl-tRNA synthetase (MetRS) from Acinetobacter baumannii with bound L-Methionine
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H18 H21 D126 K129 S172 S175 K330 K333
Catalytic site (residue number reindexed from 1) H18 H21 D126 K129 S172 S175 K330 K333
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 ZN B C142 C145 C155 C158 C142 C145 C155 C158
BS02 MET B L10 Y12 D49 W251 P255 Y258 L10 Y12 D49 W251 P255 Y258
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:5urb, PDBe:5urb, PDBj:5urb
PDBsum5urb
PubMed
UniProtA0A0D5YKJ7

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