Structure of PDB 1zq1 Chain A

Receptor sequence
>1zq1A (length=437) Species: 29292 (Pyrococcus abyssi) [Search protein sequence]
RVDEFLKERNINVGDFVRITKEEDGEEVTYEGYIMPPYELSAGDTLVLKL
ENGYNIGIALEKIRRIEVLERAKVKPEVHFEALIEGKPGLPEVTIIGTGG
TIASRIDYETGAVYPAFTAEELAKALPEIFEVANVKPKLLFNIFSEDMKP
KHWVKIAHEVAKALNSGDYGVVVAHGTDTMGYTAAALSFMLRNLGKPVVL
VGAQRSSDRPSSDAAMNLICSVRMATSEVAEVMVVMHGETGDTYCLAHRG
TKVRKMHTSRRDAFRSINDVPIAKIWPNGEIEFLRKDYRKRSDEEVEVDD
KIEEKVALVKVYPGISSEIIDFLVDKGYKGIVIEGTGLGHTPNDIIPSIE
RAVEEGVAVCMTSQCIYGRVNLNVYSTGRKLLKAGVIPCEDMLPETAYVK
LMWVLGHTQNLEEVRKMMLTNYAGEITPYTRFDTYLR
3D structure
PDB1zq1 Structural Basis for tRNA-Dependent Amidotransferase Function
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.-
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 ASP A F145 S146 E147 T178 D179 F144 S145 E146 T177 D178
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

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Molecular Function
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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)

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