Research workbench

Apo saccharopine reductase

Analyse Apo saccharopine reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FF9
Type: protein
Length: 447 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Saccharopine reductase
EC: 1.5.1.7
UniProt: Q9P4R4
Ligands: SO4
Pockets: 6 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Saccharopine reductase (EC 1.5.1.7)	protein	447	38% helix, 23% strand	Q9P4R4

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

6 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	623	0.72	0.79	55	SO4
2	135	0.48	0.78	29	empty
3	152	0.45	0.76	23	empty
4	155	0.42	0.74	26	empty
5	124	0.40	0.74	18	empty

Compared structures

1FF9 · Apo saccharopine reductase · the same entry in another collection · chain A against A, TM-score 1.00
Q9P4R4 · AlphaFold monomer V2.0 prediction for saccharopine dehydrogenase [NADP(+)… · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q9P4R4
Elsewhere: RCSB PDB 1FF9 · PDBe 1FF9 · UniProt Q9P4R4

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