MolNFT v1 · #158398 · protein

An unexpected intermediate in the reaction catalyzed by quinolinate synthase

6NSO · Quinolinate synthase a: “An unexpected intermediate in the reaction catalyzed by quinolinate synthase”. X-ray diffraction, 2 ligands (13P, SF4), 2 pockets (best druggability 0.77). MolNFT v1 #158398 on GenesisL1: 3D structure…

PDB: 6NSO
Type: protein
Length: 299 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Quinolinate synthase a
EC: 2.5.1.72
UniProt: O57767
Ligands: 13P, SF4
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Quinolinate synthase a (EC 2.5.1.72)	protein	299	44% helix, 16% strand	O57767

Ligands and binding sites

13P · 1,3-dihydroxyacetonephosphate · ligand · chains A
SF4 · Iron/sulfur cluster · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	102	0.77	0.97	32	13P, SF4
2	67	0.31	0.74	19	empty

Compared structures

6NSO · An Unexpected Intermediate in the Reaction Catalyzed by Quinolinate Synthase · the same entry in another collection · chain A against A, TM-score 1.00
O57767 · AlphaFold monomer V2.0 prediction for quinolinate synthase a (O57767) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O57767
Elsewhere: RCSB PDB 6NSO · PDBe 6NSO · UniProt O57767

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