Structure of PDB 3m4p Chain C

Receptor sequence
>3m4pC (length=429) Species: 5759 (Entamoeba histolytica) [Search protein sequence]
TPIVCNIRDAAGLEGKLVTFKGWAYHIRKARKTLIFVELRDGSGYCQCVI
FGKELCEPEKVKLLTRECSLEITGRLNAYAGKNHPPEIADILNLEMQVTE
WKVIGESPIDLENIINKDSSIPQKMQNRHIVIRSEHTQQVLQLRSEIQWY
FRKYYHDNHFTEIQPPTIVKTLFKLQYFNEPAYLTQSSQLYLESVIASLG
KSFCMLSSYRAEQSRTVRHLAEYLHLEAELPFISFEDLLNHLEDLVCTVI
DNVMAVHGDKIRKMNPHLKLPTRPFKRMTYADAIKYCNDHDKPFEYGEDI
SEKPERQMTDEIGCPIFMIHFPSKMKAFYMSKVPGHPDLTESVDLLMPGV
GEIVGGSMRIWNYDELMGAYKANGLNPDPYYWYTQQRKYGSCPHGGYGLG
VERLVMWLLGEDHIRKVCLYPRYLERCEP
3D structure
PDB3m4p X-ray crystal structure of asparaginyl-tRNA synthetase from the eukaryotic human pathogen Entamoeba histolytica.
ChainC
Resolution2.83 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R227 E229 R235 H236 E374 G377 R425
Catalytic site (residue number reindexed from 1) R210 E212 R218 H219 E352 G355 R403
Enzyme Commision number 6.1.1.22: asparagine--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 4AD C S204 Q206 R227 R235 H236 L237 Y240 H242 E244 E374 I375 R381 Y419 G420 R425 S187 Q189 R210 R218 H219 L220 Y223 H225 E227 E352 I353 R359 Y397 G398 R403
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004816 asparagine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006421 asparaginyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:3m4p, PDBe:3m4p, PDBj:3m4p
PDBsum3m4p
PubMed
UniProtC4LWW8

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