Structure of PDB 6c86 Chain B

Receptor sequence
>6c86B (length=497) Species: 353152 (Cryptosporidium parvum Iowa II) [Search protein sequence]
SHYTDNRYKMMECIKDAGRPFYPHKFKISMSLPAYALKYGNVENGYIDKD
TTLSLSGRVTSIRSSSSKLIFYDIFCEEQKVQIIANIMEHDISTGEFSVS
HSEIRRGDVVGFTGFPGKSKRGELSLFSKSVVLLSPCYHMLPTAIDQEVR
YRQRYLDLMLNEESRKVFKLRSRAIKYIRNYFDRLGFLEVETPMLNMIYG
GAAARPFITYHNELETQLYMRIAPELYLKQLIVGGLDKVYEIGKNFRNEG
IDLTHNPEFTAMEFYMAYADYYDLMDLTEELISGLVLEIHGSLKIPYHPD
GPEGKCIEIDFTTPWKRFSFVEEIESGLGEKLKRPLDSQENIDFMVEMCE
KHEIELPHPRTAAKLLDKLAGHFVETKCTNPSFIIDHPQTMSPLAKWHRE
KPEMTERFELFVLGKELCNAYTELNEPLQQRKFFEQQADAKASGDVEACP
IDETFCLALEHGLPPTGGWGLGIDRLIMFLADKNNIKEVILFPAMRN
3D structure
PDB6c86 Crystal Structure of Lysyl-tRNA Synthetase from Cryptosporidium parvum complexed with L-Lysylsulfamoyl Adenosine
ChainB
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R295 E297 T302 H303 E464 N467 R523
Catalytic site (residue number reindexed from 1) R247 E249 T254 H255 E416 N419 R475
Enzyme Commision number 6.1.1.6: lysine--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 KAA B G249 A271 E273 R295 T302 H303 N304 F307 E311 Y313 E464 L465 N467 Y469 E471 G516 W517 G518 G520 R523 G201 A223 E225 R247 T254 H255 N256 F259 E263 Y265 E416 L417 N419 Y421 E423 G468 W469 G470 G472 R475
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004824 lysine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006430 lysyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6c86, PDBe:6c86, PDBj:6c86
PDBsum6c86
PubMed
UniProtQ5CR27

[Back to BioLiP]