Research workbench

Sinapyl alcohol dehydrogenase at 2.5 ångström resolution

Analyse Sinapyl alcohol dehydrogenase at 2.5 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YQX
Type: protein
Length: 718 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sinapyl alcohol dehydrogenase
EC: 1.1.1.195
UniProt: Q94G59
Ligands: NAP, ZN
Pockets: 6 · best druggability 0.79

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Sinapyl alcohol dehydrogenase (EC 1.1.1.195)	protein	359	28% helix, 28% strand	Q94G59

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 4 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	716	0.79	0.83	86	NAP
2	615	0.79	0.84	64	NAP
3	67	0.71	0.96	20	empty
4	52	0.69	0.98	15	empty
5	100	0.37	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 1329 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1YQX · Sinapyl Alcohol Dehydrogenase at 2.5 Angstrom Resolution · 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 Q94G59
Elsewhere: RCSB PDB 1YQX · PDBe 1YQX · UniProt Q94G59

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