Structure of PDB 3sp1 Chain B

Receptor sequence
>3sp1B (length=439) Species: 139 (Borreliella burgdorferi) [Search protein sequence]
SMILKLYNTRTKDFSELTNFENVKVYACGPTVYNYAHIGNFRTYIFGDLL
IKTLRFLGYKVNYAMNITDIGHGLTVYEISEFFTEAFFNDCRKLNIVYPD
KVLVASKHIPIMIEVVKILEEKKITYFSNGNVYFDTSCFKSYGEMAGIKF
KRNKTDFVLWFTNSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKDAL
DIHLGGVDHIGVHHINEIAIAECFLNKKWCDVFVHGEFLIMDYNKMSFIT
VKDLEDQNFSPLDFRYLCLTSHYRNQLKFSLDNLQASKIARENLINKLSY
FYESLDPVDLNTLNKDLKNFGFSVEKEYYDSFVEKISFDLNVAQGLALLW
EIIKSDNLSFVSKLRLAFIFDEIMSLNLREEILKNLQNHDVVIDENMKAL
IEERRIAKCEKNFKRADEIRDFFAKKGFVLVDGTKVKRG
3D structure
PDB3sp1 Ligand co-crystallization of aminoacyl-tRNA synthetases from infectious disease organisms.
ChainB
Resolution2.55 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.16: cysteine--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 C27 C221 H246 C28 C188 H213
BS02 AMP B G38 N39 T42 Y43 G239 H242 F271 L272 K278 M279 G39 N40 T43 Y44 G206 H209 F238 L239 K245 M246
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004817 cysteine-tRNA ligase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006423 cysteinyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:3sp1, PDBe:3sp1, PDBj:3sp1
PDBsum3sp1
PubMed28303005
UniProtO51545|SYC_BORBU Cysteine--tRNA ligase (Gene Name=cysS)

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