Structure of PDB 6gq3 Chain A Binding Site BS01

Receptor Information
>6gq3 Chain A (length=509) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
CGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLA
VVDPLFGMQPIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEII
LHLYDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTE
DGFLAVCSEAKGLVTLKHSATPFLKVEPFLPGHYEVLDLKPNGKVASVEM
VKYHHCRDVFPGFEIETVKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDS
SLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVADHIGSEHYEV
LFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIFS
GEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHG
LELRVPFLDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEIL
WRPSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHY
PGRADWLSH
Ligand information
Ligand IDONL
InChIInChI=1S/C6H11NO3/c1-4(8)2-3-5(7)6(9)10/h5H,2-3,7H2,1H3,(H,9,10)/t5-/m0/s1
InChIKeyKSIJECNNZVKMJG-YFKPBYRVSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=O)CC[C@@H](C(=O)O)N
ACDLabs 10.04O=C(CCC(N)C(=O)O)C
OpenEye OEToolkits 1.5.0CC(=O)CCC(C(=O)O)N
CACTVS 3.341CC(=O)CC[CH](N)C(O)=O
CACTVS 3.341CC(=O)CC[C@H](N)C(O)=O
FormulaC6 H11 N O3
Name5-OXO-L-NORLEUCINE
ChEMBL
DrugBankDB04296
ZINCZINC000000895890
PDB chain6gq3 Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6gq3 High-resolution crystal structure of human asparagine synthetase enables analysis of inhibitor binding and selectivity.
Resolution1.85 Å
Binding residue
(original residue number in PDB)		C1 R48 V51 V52 Y73 N74 G75 E76 V95 D96
Binding residue
(residue number reindexed from 1)		C1 R48 V51 V52 Y73 N74 G75 E76 V95 D96
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) W4 L49 N74 G75 T336 R339
Catalytic site (residue number reindexed from 1) W4 L49 N74 G75 T324 R327
Enzyme Commision number 6.3.5.4: asparagine synthase (glutamine-hydrolyzing).
Gene Ontology
Molecular Function
GO:0004066 asparagine synthase (glutamine-hydrolyzing) activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006529 asparagine biosynthetic process
GO:0006541 glutamine metabolic process
GO:0042149 cellular response to glucose starvation
GO:0043066 negative regulation of apoptotic process
GO:0045931 positive regulation of mitotic cell cycle
GO:0070981 L-asparagine biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6gq3, PDBe:6gq3, PDBj:6gq3
PDBsum6gq3
PubMed31552298
UniProtP08243|ASNS_HUMAN Asparagine synthetase [glutamine-hydrolyzing] (Gene Name=ASNS)

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