Structure of PDB 6nsu Chain A

Receptor sequence
>6nsuA (length=298) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence]
DLVEEILRLKEERNAIILAHNYQLPEVQDIADFIGDSLELARRATRVDAD
VIVFAGVDFMAETAKILNPDKVVLIPSREATCAMANMLKVEHILEAKRKY
PNAPVVLYVNSTAEAKAYADVTVTSANAVEVVKKLDSDVVIFGPDKNLAH
YVAKMTGKKIIPVPSKGHCYVHQKFTLDDVERAKKLHPNAKLMIHPECIP
EVQEKADIIASTGGMIKRACEWDEWVVFTEREMVYRLRKLYPQKKFYPAR
EDAFCIGMKAITLKNIYESLKDMKYKVEVPEEIARKARKAIERMLEMS
3D structure
PDB6nsu An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase.
ChainA
Resolution2.15 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 C83 C170 C256 C82 C169 C255
BS02 DYA A H21 Y23 N111 H196 E198 T213 H20 Y22 N110 H195 E197 T212
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:6nsu, PDBe:6nsu, PDBj:6nsu
PDBsum6nsu
PubMed31390192
UniProtO57767|NADA_PYRHO Quinolinate synthase (Gene Name=nadA)

[Back to BioLiP]