Structure of PDB 1evk Chain A Binding Site BS01

Receptor Information

>1evk Chain A (length=401) Species: 562 (Escherichia coli)

RDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQ
EVKGPFMMDRVLWEKTGHWDNYKDAMFTTSSENREYCIKPMNCPGHVQIF
NQGLKSYRDLPLRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEE
QIRDEVNGCIRLVYDMYSTFGFEKIVVKLSTRPEKRIGSDEMWDRAEADL
AVALEENNIPFEYQLGEGAFYGPKIEFTLYDCLDRAWQCGTVQLDFSLPS
RLSASYVGEDNERKVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPVQ
VVIMNITDSQSEYVNELTQKLSNAGIRVKADLRNEKIGFKIREHTLRRVP
YMLVCGDKEVESGKVAVRTRRGKDLGSMDVNEVIEKLQQEIRSRSLKQLE
E

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 1evk Chain A Residue 1

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1evk Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase.
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): C334 H385 H511
• Binding residue (residue number reindexed from 1): C93 H144 H270
• Annotation score: 1

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.

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

External links

• PDB: RCSB:1evk, PDBe:1evk, PDBj:1evk
• PDBsum: 1evk
• PubMed: 10881191
• UniProt: P0A8M3|SYT_ECOLI Threonine--tRNA ligase (Gene Name=thrS)