MolNFT v1 · #118482 · protein

Structure of quinolinate synthase in complex with citrate

5F35 · Quinolinate synthase a: “Structure of quinolinate synthase in complex with citrate”. X-ray diffraction, 2 ligands (SF4, MG), 2 pockets (best druggability 0.74). MolNFT v1 #118482 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 5F35
Type: protein
Length: 303 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: Q9X1X7
Ligands: SF4, MG
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Quinolinate synthase a (EC 2.5.1.72)	protein	303	47% helix, 16% strand	Q9X1X7

Ligands and binding sites

SF4 · Iron/sulfur cluster · ligand · chains A
MG · Magnesium ion · metal · chains A
FLC · Citrate anion · additive · 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	120	0.74	0.94	31	SF4, FLC
2	51	0.39	0.81	17	empty

Compared structures

5F35 · Structure of quinolinate synthase in complex with citrate · the same entry in another collection · chain A against A, TM-score 1.00
Q9X1X7 · AlphaFold monomer V2.0 prediction for quinolinate synthase a (Q9X1X7) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9X1X7
Elsewhere: RCSB PDB 5F35 · PDBe 5F35 · UniProt Q9X1X7

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