Structure of PDB 1evk Chain A

Receptor sequence
>1evkA (length=401) Species: 562 (Escherichia coli) [Search protein sequence]
RDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQ
EVKGPFMMDRVLWEKTGHWDNYKDAMFTTSSENREYCIKPMNCPGHVQIF
NQGLKSYRDLPLRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEE
QIRDEVNGCIRLVYDMYSTFGFEKIVVKLSTRPEKRIGSDEMWDRAEADL
AVALEENNIPFEYQLGEGAFYGPKIEFTLYDCLDRAWQCGTVQLDFSLPS
RLSASYVGEDNERKVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPVQ
VVIMNITDSQSEYVNELTQKLSNAGIRVKADLRNEKIGFKIREHTLRRVP
YMLVCGDKEVESGKVAVRTRRGKDLGSMDVNEVIEKLQQEIRSRSLKQLE
E
3D structure
PDB1evk Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C334 R363 Q381 D383 H385 K465 H511
Catalytic site (residue number reindexed from 1) C93 R122 Q140 D142 H144 K224 H270
Enzyme Commision number 6.1.1.3: threonine--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 A C334 H385 H511 C93 H144 H270
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004829 threonine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006435 threonyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1evk, PDBe:1evk, PDBj:1evk
PDBsum1evk
PubMed10881191
UniProtP0A8M3|SYT_ECOLI Threonine--tRNA ligase (Gene Name=thrS)

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