Structure of PDB 5kts Chain A Binding Site BS02

Receptor Information
>5kts Chain A (length=303) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSFTMDLVEEILRLKEERNAIILAHNYQLPEVQDIADFIGDSLELARRAT
RVDADVIVFAGVDFMAETAKILNPDKVVLIPSREATCAMANMLKVEHILE
AKRKYPNAPVVLYVNSTAEAKAYADVTVTSANAVEVVKKLDSDVVIFGPD
KNLAHYVAKMTGKKIIPVPSKGHCYVHQKFTLDDVERAKKLHPNAKLMIH
PECIPEVQEKADIIASTGGMIKRACEWDEWVVFTEREMVYRLRKLYPQKK
FYPAREDAFCIGMKAITLKNIYESLKDMKYKVEVPEEIARKARKAIERML
EMS
Ligand information
Ligand IDCIZ
InChIInChI=1S/C5H6O4/c1-3(5(8)9)2-4(6)7/h2H,1H3,(H,6,7)(H,8,9)/b3-2-
InChIKeyHNEGQIOMVPPMNR-IHWYPQMZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6CC(=CC(=O)O)C(=O)O
OpenEye OEToolkits 1.7.6C/C(=C/C(=O)O)/C(=O)O
CACTVS 3.385CC(=C/C(O)=O)/C(O)=O
ACDLabs 12.01O=C(O)C(C)=[C@H]C(O)=O
CACTVS 3.385CC(=CC(O)=O)C(O)=O
FormulaC5 H6 O4
Name(~{Z})-2-methylbut-2-enedioic acid;
CITRACONATE
ChEMBL
DrugBankDB04734
ZINCZINC000003860287
PDB chain5kts Chain A Residue 402 [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]
PDB5kts Crystal Structures of the Iron-Sulfur Cluster-Dependent Quinolinate Synthase in Complex with Dihydroxyacetone Phosphate, Iminoaspartate Analogues, and Quinolinate.
Resolution1.34 Å
Binding residue
(original residue number in PDB)		H21 Y23 D37 S38 Y109 T125 S126 H196 S212 T213
Binding residue
(residue number reindexed from 1)		H25 Y27 D41 S42 Y113 T129 S130 H200 S216 T217
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5kts, PDBe:5kts, PDBj:5kts
PDBsum5kts
PubMed27404889
UniProtO57767|NADA_PYRHO Quinolinate synthase (Gene Name=nadA)

[Back to BioLiP]