Structure of PDB 3c9q Chain A Binding Site BS02

Receptor Information
>3c9q Chain A (length=195) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AVHYQPASPPRDACVYSSCYCEENVWKLCEYIKNHDQYPLEECYAVFISN
ERKMIPIWKQQARPGDGPVIWDYHVVLLHVSSGGQSFIYDLDTVLPFPCL
FDTYVEDAIKSDDDIHPQFRRKFRVICADSYLKNFASDRSHMKDSSGNWR
EPPPPYPCIETGDSKMNLNDFISMDPKVGWGAVYTLSEFTHRFGS
Ligand information
Ligand IDCO3
InChIInChI=1S/CH2O3/c2-1(3)4/h(H2,2,3,4)/p-2
InChIKeyBVKZGUZCCUSVTD-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(=O)([O-])[O-]
ACDLabs 10.04
CACTVS 3.341		[O-]C([O-])=O
FormulaC O3
NameCARBONATE ION
ChEMBL
DrugBankDB14531
ZINC
PDB chain3c9q Chain A Residue 211 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3c9q Crystal structure of the uncharacterized human protein C8orf32 with bound peptide.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		V132 R199
Binding residue
(residue number reindexed from 1)		V125 R192
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.1.122: protein N-terminal glutamine amidohydrolase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008418 protein-N-terminal asparagine amidohydrolase activity
GO:0016787 hydrolase activity
GO:0016811 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
GO:0070773 protein-N-terminal glutamine amidohydrolase activity
Biological Process
GO:0036211 protein modification process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
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:3c9q, PDBe:3c9q, PDBj:3c9q
PDBsum3c9q
PubMed
UniProtQ96HA8|NTAQ1_HUMAN Protein N-terminal glutamine amidohydrolase (Gene Name=NTAQ1)

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