Structure of PDB 4oud Chain A

Receptor sequence
>4oudA (length=411) Species: 1403831 (Escherichia coli str. K-12 substr. MC4100) [Search protein sequence]
SNLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTADSLHAGHLV
PLLCLKRFQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEETVQEWVDK
IRKQVAPFLDFDCGENSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMIN
KEAVKQRLNREDQGISFTEFSYNLLQGYDFACLNKQYGVVLQIGGSDQWG
NITSGIDLTRRLHQNQVFGLTVPLITKAGAVWLDPKKTSPYKFYQFAINA
ADADVYRWLKFGTFMSIEEINALEEEDKNSGKAPRAQYVFAEQVTRLVHG
EEGLQAAKRITECLFSGSLSALSEADFEQLAQDGVPMVEMEKGADLMQAL
VDSELQPSRGQARKTIASNAITINGEKQSDPEYFFKEEDRLFGRFTLLRR
GKKNYCLICWK
3D structure
PDB4oud Biocontainment of genetically modified organisms by synthetic protein design.
ChainA
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T43 H48 H51 K85 R89 Q179 D200
Catalytic site (residue number reindexed from 1) T40 H45 H48 K82 R86 Q176 D197
Enzyme Commision number 6.1.1.1: tyrosine--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 TYR A Y37 G39 D41 L71 T76 D81 Y175 Q179 D182 Q201 Y34 G36 D38 L68 T73 D78 Y172 Q176 D179 Q198
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003723 RNA binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004831 tyrosine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006437 tyrosyl-tRNA aminoacylation
GO:0043039 tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4oud, PDBe:4oud, PDBj:4oud
PDBsum4oud
PubMed25607366
UniProtA0A0H2UKY9

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