Structure of PDB 5kto Chain A

Receptor sequence
>5ktoA (length=298) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence]
DLVEEILRLKEERNAIILAHNYQLPEVQDIADFIGDSLELARRATRVDAD
VIVFAGVDFMAETAKILNPDKVVLIPSREATCAMANMLKVEHILEAKRKY
PNAPVVLYVNSTAEAKAYADVTVTSANAVEVVKKLDSDVVIFGPDKNLAH
YVAKMTGKKIIPVPSKGHCYVHQKFTLDDVERAKKLHPNAKLMIHPECIP
EVQEKADIIASTGGMIKRACEWDEWVVFTEREMVYRLRKLYPQKKFYPAR
EDAFCIGMKAITLKNIYESLKDMKYKVEVPEEIARKARKAIERMLEMS
3D structure
PDB5kto Crystal Structures of the Iron-Sulfur Cluster-Dependent Quinolinate Synthase in Complex with Dihydroxyacetone Phosphate, Iminoaspartate Analogues, and Quinolinate.
ChainA
Resolution1.442 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.72: quinolinate synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SF4 A Y23 C83 C170 C256 Y22 C82 C169 C255
BS02 NTM A H21 Y23 D37 S38 M61 Y109 H173 H196 E198 H20 Y22 D36 S37 M60 Y108 H172 H195 E197
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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Cellular Component
External links
PDB RCSB:5kto, PDBe:5kto, PDBj:5kto
PDBsum5kto
PubMed27404889
UniProtO57767|NADA_PYRHO Quinolinate synthase (Gene Name=nadA)

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