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Apo histidine-tagged saccharopine dehydrogenase (L-glu forming) from saccharomyces cerevisiae

Analyse Apo histidine-tagged saccharopine dehydrogenase (L-glu forming) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AXQ
Type: protein
Length: 445 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Saccharopine dehydrogenase
EC: 1.5.1.10
UniProt: P38999
Ligands: SO4
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Saccharopine dehydrogenase (EC 1.5.1.10)	protein	445	40% helix, 24% strand	P38999

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A

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

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	782	0.70	0.76	75	SO4
2	56	0.34	0.77	17	empty

Compared structures

2AXQ · Apo histidine-tagged saccharopine dehydrogenase (L-Glu forming) from Saccharomyces… · the same entry in another collection · chain A against A, TM-score 1.00
P38999 · AlphaFold monomer V2.0 prediction for saccharopine dehydrogenase [NADP(+)… · a predicted model of the same protein · chain A against A, TM-score 0.90

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 P38999
Elsewhere: RCSB PDB 2AXQ · PDBe 2AXQ · UniProt P38999

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