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Glutamate dehydrogenase

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

PDB: 1AUP
Type: protein
Length: 427 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD-specific glutamate dehydrogenase
EC: 1.4.1.2
UniProt: P24295
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD-specific glutamate dehydrogenase (EC 1.4.1.2)	protein	427	50% helix, 17% strand	P24295

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	699	0.73	0.79	63	empty
2	159	0.54	0.80	23	empty
3	52	0.37	0.80	14	empty

Compared structures

1AUP · Glutamate dehydrogenase · the same entry in another collection · chain A against A, TM-score 1.00
P24295 · AlphaFold monomer V2.0 prediction for NAD-specific glutamate dehydrogenase (P24295) · 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 P24295
Elsewhere: RCSB PDB 1AUP · PDBe 1AUP · UniProt P24295

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