Structure of PDB 6nsu Chain A Binding Site BS02

Receptor Information
>6nsu Chain A (length=298) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DLVEEILRLKEERNAIILAHNYQLPEVQDIADFIGDSLELARRATRVDAD
VIVFAGVDFMAETAKILNPDKVVLIPSREATCAMANMLKVEHILEAKRKY
PNAPVVLYVNSTAEAKAYADVTVTSANAVEVVKKLDSDVVIFGPDKNLAH
YVAKMTGKKIIPVPSKGHCYVHQKFTLDDVERAKKLHPNAKLMIHPECIP
EVQEKADIIASTGGMIKRACEWDEWVVFTEREMVYRLRKLYPQKKFYPAR
EDAFCIGMKAITLKNIYESLKDMKYKVEVPEEIARKARKAIERMLEMS
Ligand information
Ligand IDDYA
InChIInChI=1S/C4H5NO4/c5-2(4(8)9)1-3(6)7/h1H,5H2,(H,6,7)(H,8,9)/b2-1-
InChIKeyABZHGLSYGDUSDL-UPHRSURJSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C(=C(/C(=O)O)\N)\C(=O)O
OpenEye OEToolkits 1.7.6C(=C(C(=O)O)N)C(=O)O
CACTVS 3.385NC(=CC(O)=O)C(O)=O
CACTVS 3.385N\C(=C/C(O)=O)C(O)=O
FormulaC4 H5 N O4
NameDIDEHYDROASPARTATE
ChEMBL
DrugBank
ZINC
PDB chain6nsu Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6nsu An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase.
Resolution2.15 Å
Binding residue
(original residue number in PDB)		H21 Y23 N111 H196 E198 T213
Binding residue
(residue number reindexed from 1)		H20 Y22 N110 H195 E197 T212
Annotation score1
Enzymatic activity
Enzyme Commision number 2.5.1.72: quinolinate synthase.
Gene Ontology
Molecular Function
GO:0008987 quinolinate synthetase A activity
GO:0016740 transferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process
GO:0019805 quinolinate biosynthetic process
GO:0034628 'de novo' NAD biosynthetic process from aspartate
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6nsu, PDBe:6nsu, PDBj:6nsu
PDBsum6nsu
PubMed31390192
UniProtO57767|NADA_PYRHO Quinolinate synthase (Gene Name=nadA)

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