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Apo and holo structures of an NADP(H)-dependent cinnamyl alcohol dehydrogenase from saccharomyces cerevisiae

Analyse Apo and holo structures of an NADP(H)-dependent cinnamyl alcohol dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Q1N
Type: protein
Length: 360 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical zinc-type alcohol dehydrogenase- like protein in PRE5-FET4 intergenic region
UniProt: Q04894
Ligands: ZN
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical zinc-type alcohol dehydrogenase- like protein in PRE5-FET4 intergenic region	protein	360	28% helix, 26% strand	Q04894

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

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	506	0.72	0.81	57	empty

Compared structures

1Q1N · Apo and holo structures of an NADP(H)-dependent cinnamyl alcohol dehydrogenase from… · the same entry in another collection · chain A against A, TM-score 1.00
Q04894 · AlphaFold monomer V2.0 prediction for NADP-dependent alcohol dehydrogenase 6 (Q04894) · 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 Q04894
Elsewhere: RCSB PDB 1Q1N · PDBe 1Q1N · UniProt Q04894

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