Structure of PDB 1cg3 Chain A Binding Site BS02

Receptor Information
>1cg3 Chain A (length=431) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GNNVVVLGTQWGDEGKGKIVDLLTERAKYVVRYQGGHNAGHTLVINGEKT
VLHLIPSGILRENVTSIIGNGVVLSPAALMKEMKELEDRGIPVRERLLLS
EACPLILDYHVALDNAREKARGAKAIGTTGRGIGPAYEDKVALRGLRVGD
LFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVADILTSM
VVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVAT
GSGLGPRYVDYVLGILKAYSTRVGAGPFPTELFDETGEFLCKQGNEFGAT
TGRRRRTGWLDTVAVRRAVQLNSLSGFCLTKLDVLDGLKEVKLCVAYRMP
DGREVTTTPLAADDWKGVEPIYETMPGWSESTFGVKDRSGLPQAALNYIK
RIEELTGVPIDIISTGPDRTETMILRDPFDA
Ligand information
Ligand IDHDA
InChIInChI=1S/C3H5NO4/c5-2-4(8)1-3(6)7/h2,8H,1H2,(H,6,7)
InChIKeyURJHVPKUWOUENU-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.370ON(CC(O)=O)C=O
ACDLabs 12.01O=C(O)CN(O)C=O
OpenEye OEToolkits 1.7.0C(C(=O)O)N(C=O)O
FormulaC3 H5 N O4
NameHADACIDIN
ChEMBLCHEMBL331373
DrugBankDB02109
ZINCZINC000001482078
PDB chain1cg3 Chain A Residue 437 [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]
PDB1cg3 Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		D13 G40 G298 T300 T301 R303 R305
Binding residue
(residue number reindexed from 1)		D13 G40 G298 T300 T301 R303 R305
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D13 K16 G40 H41 Q224
Catalytic site (residue number reindexed from 1) D13 K16 G40 H41 Q224
Enzyme Commision number 6.3.4.4: adenylosuccinate synthase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0004019 adenylosuccinate synthase activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
GO:0097216 guanosine tetraphosphate binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006974 DNA damage response
GO:0015949 nucleobase-containing small molecule interconversion
GO:0044208 'de novo' AMP biosynthetic process
GO:0046040 IMP metabolic process
GO:0046086 adenosine biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1cg3, PDBe:1cg3, PDBj:1cg3
PDBsum1cg3
PubMed10346917
UniProtP0A7D4|PURA_ECOLI Adenylosuccinate synthetase (Gene Name=purA)

[Back to BioLiP]