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Crystal structure of the quinate dehydrogenase from corynebacterium glutamicum

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

PDB: 2NLO
Type: protein
Length: 281 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Shikimate dehydrogenase
EC: 1.1.1.25
UniProt: Q9X5C9
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Shikimate dehydrogenase (EC 1.1.1.25)	protein	281	40% helix, 20% strand	Q9X5C9

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

3 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	521	0.71	0.80	48	GOL
2	64	0.30	0.74	14	empty
3	51	0.27	0.74	16	empty

Compared structures

2NLO · Crystal Structure of the Quinate Dehydrogenase from Corynebacterium glutamicum · 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 2NLO · PDBe 2NLO · UniProt Q9X5C9

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