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Quinate dehydrogenase from corynebacterium glutamicum in complex with NAD

Analyse Quinate dehydrogenase from corynebacterium glutamicum in complex with NAD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3JYO
Type: protein
Length: 282 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: QUINATE/SHIKIMATE dehydrogenase
EC: 1.1.1.24, 1.1.1.-
UniProt: Q9X5C9
Ligands: NAD
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	QUINATE/SHIKIMATE dehydrogenase (EC 1.1.1.24, 1.1.1.-)	protein	282	40% helix, 18% strand	Q9X5C9

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · 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	535	0.67	0.78	46	NAD
2	50	0.29	0.75	15	empty

Compared structures

3JYO · Quinate dehydrogenase from Corynebacterium glutamicum in complex with NAD · the same entry in another collection · chain A against A, TM-score 1.00
Q9X5C9 · AlphaFold monomer V2.0 prediction for QUINATE/SHIKIMATE dehydrogenase (NAD(+)) (Q9X5C9) · 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 Q9X5C9
Elsewhere: RCSB PDB 3JYO · PDBe 3JYO · UniProt Q9X5C9

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