Structure of PDB 1x55 Chain A Binding Site BS01

Receptor Information
>1x55 Chain A (length=434) Species: 53953 (Pyrococcus horikoshii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIEKVYCQEVKPELDGKKVRLAGWVYTNMRVGKKIFLWIRDSTGIVQAVV
AKNVVGEETFEKAKKLGRESSVIVEGIVKADERAPGGAEVHVEKLEVIQA
VSEFPIPENPEQASPELLLDYRHLHIRTPKASAIMKVKETLIMAAREWLL
KDGWHEVFPPILVTGAVEGGATLFKLKYFDKYAYLSQSAQLYLEAAIFGL
EKVWSLTPSFRAEKSRTRRHLTEFWHLELEAAWMDLWDIMKVEEELVSYM
VQRTLELRKKEIEMFRDDLTTLKNTEPPFPRISYDEAIDILQSKGVNVEW
GDDLGADEERVLTEEFDRPFFVYGYPKHIKAFYMKEDPNDPRKVLASDML
APEGYGEIIGGSQREDDYDKLLNRILEEGMDPKDYEWYLDLRRYGSVPHS
GFGLGVERLVAWVLKLDHIRWAALFPRTPARLYP
Ligand information
Ligand IDNSS
InChIInChI=1S/C14H20N8O8S/c15-5(1-7(16)23)13(26)21-31(27,28)29-2-6-9(24)10(25)14(30-6)22-4-20-8-11(17)18-3-19-12(8)22/h3-6,9-10,14,24-25H,1-2,15H2,(H2,16,23)(H,21,26)(H2,17,18,19)/p+1/t5-,6+,9+,10+,14+/m0/s1
InChIKeyMOAVDHSPHZUJSX-UFIIOMENSA-O
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(N)CC(C(=O)NS(=O)(=O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O)[NH3+]
CACTVS 3.341NC(=O)C[CH]([NH3+])C(=O)N[S](=O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COS(=O)(=O)NC(=O)[C@H](CC(=O)N)[NH3+])O)O)N
CACTVS 3.341NC(=O)C[C@H]([NH3+])C(=O)N[S](=O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COS(=O)(=O)NC(=O)C(CC(=O)N)[NH3+])O)O)N
FormulaC14 H21 N8 O8 S
Name5'-O-[N-(L-ASPARAGINYL)SULFAMOYL]ADENOSINE;
ASN-SA
ChEMBL
DrugBank
ZINC
PDB chain1x55 Chain A Residue 3002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1x55 Structural Basis of the Water-assisted Asparagine Recognition by Asparaginyl-tRNA Synthetase.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		E168 S188 Q190 R211 H220 L221 F224 H226 E228 E357 I358 I359 R364 F402 G403 G405 R408
Binding residue
(residue number reindexed from 1)		E168 S188 Q190 R211 H220 L221 F224 H226 E228 E357 I358 I359 R364 F402 G403 G405 R408
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) R211 E213 R219 H220 E357 G360 R408
Catalytic site (residue number reindexed from 1) R211 E213 R219 H220 E357 G360 R408
Enzyme Commision number 6.1.1.22: asparagine--tRNA ligase.
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1x55, PDBe:1x55, PDBj:1x55
PDBsum1x55
PubMed16753178
UniProtO57980|SYN_PYRHO Asparagine--tRNA ligase (Gene Name=asnS)

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