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Crystal structure of saccharopine dehydrogenase from saccharomyces cerevisiae

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

PDB: 2Q99
Type: protein
Length: 372 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Saccharopine dehydrogenase [NAD+, L-lysine-forming
EC: 1.5.1.7
UniProt: P38998
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Saccharopine dehydrogenase [NAD+, L-lysine-forming (EC 1.5.1.7)	protein	372	37% helix, 13% strand	P38998

Pockets

2 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	437	0.62	0.76	40	empty
2	90	0.45	0.80	22	empty

Modifications

Observed in the structure: 3 modified, 1 disulfide (engineered, disulfide).

Compared structures

2Q99 · Crystal Structure of Saccharopine Dehydrogenase from Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
P38998 · AlphaFold monomer V2.0 prediction for saccharopine dehydrogenase [NAD(+)… · 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 P38998
Elsewhere: RCSB PDB 2Q99 · PDBe 2Q99 · UniProt P38998

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