Structure of PDB 1zq1 Chain A Binding Site BS01

Receptor Information
>1zq1 Chain A (length=437) Species: 29292 (Pyrococcus abyssi) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RVDEFLKERNINVGDFVRITKEEDGEEVTYEGYIMPPYELSAGDTLVLKL
ENGYNIGIALEKIRRIEVLERAKVKPEVHFEALIEGKPGLPEVTIIGTGG
TIASRIDYETGAVYPAFTAEELAKALPEIFEVANVKPKLLFNIFSEDMKP
KHWVKIAHEVAKALNSGDYGVVVAHGTDTMGYTAAALSFMLRNLGKPVVL
VGAQRSSDRPSSDAAMNLICSVRMATSEVAEVMVVMHGETGDTYCLAHRG
TKVRKMHTSRRDAFRSINDVPIAKIWPNGEIEFLRKDYRKRSDEEVEVDD
KIEEKVALVKVYPGISSEIIDFLVDKGYKGIVIEGTGLGHTPNDIIPSIE
RAVEEGVAVCMTSQCIYGRVNLNVYSTGRKLLKAGVIPCEDMLPETAYVK
LMWVLGHTQNLEEVRKMMLTNYAGEITPYTRFDTYLR
Ligand information
Ligand IDASP
InChIInChI=1S/C4H7NO4/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H,6,7)(H,8,9)/t2-/m0/s1
InChIKeyCKLJMWTZIZZHCS-REOHCLBHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C(C(C(=O)O)N)C(=O)O
OpenEye OEToolkits 1.7.0C([C@@H](C(=O)O)N)C(=O)O
CACTVS 3.370N[CH](CC(O)=O)C(O)=O
CACTVS 3.370N[C@@H](CC(O)=O)C(O)=O
ACDLabs 12.01O=C(O)CC(N)C(=O)O
FormulaC4 H7 N O4
NameASPARTIC ACID
ChEMBLCHEMBL274323
DrugBankDB00128
ZINCZINC000000895032
PDB chain1zq1 Chain A Residue 1000 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1zq1 Structural Basis for tRNA-Dependent Amidotransferase Function
Resolution3.0 Å
Binding residue
(original residue number in PDB)		F145 S146 E147 T178 D179
Binding residue
(residue number reindexed from 1)		F144 S145 E146 T177 D178
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) T102 A113 T178 D179 K256 G379
Catalytic site (residue number reindexed from 1) T101 A112 T177 D178 K255 G378
Enzyme Commision number 6.3.5.-
Gene Ontology
Molecular Function
GO:0004067 asparaginase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Biological Process
GO:0006412 translation
GO:0006450 regulation of translational fidelity
GO:0006520 amino acid metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1zq1, PDBe:1zq1, PDBj:1zq1
PDBsum1zq1
PubMed16216574
UniProtQ9V0T9|GATD_PYRAB Glutamyl-tRNA(Gln) amidotransferase subunit D (Gene Name=gatD)

[Back to BioLiP]