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Crystal structure of cinnamyl-alcohol dehydrogenase 2 mutant K169A

Analyse Crystal structure of cinnamyl-alcohol dehydrogenase 2 mutant K169A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QUK
Type: protein
Length: 313 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydroflavonol-4-reductase
EC: 1.1.1.-
UniProt: G7IYC1
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydroflavonol-4-reductase (EC 1.1.1.-)	protein	313	41% helix, 18% strand	G7IYC1

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	699	0.67	0.75	61	empty

Compared structures

4QUK · Crystal Structure of Cinnamyl-Alcohol Dehydrogenase 2 Mutant K169A · the same entry in another collection · chain A against A, TM-score 1.00

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 G7IYC1
Elsewhere: RCSB PDB 4QUK · PDBe 4QUK · UniProt G7IYC1

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