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Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the free enzyme

Analyse Regulation of isocitrate dehydrogenase by phosphorylation involves no… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ICD
Type: protein
Length: 414 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphorylated isocitrate dehydrogenase
EC: 1.1.1.42
UniProt: P08200
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphorylated isocitrate dehydrogenase (EC 1.1.1.42)	protein	414	40% helix, 18% strand	P08200

Pockets

3 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	363	0.62	0.77	45	empty
2	99	0.43	0.78	21	empty
3	62	0.30	0.76	17	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

4ICD · Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range… · the same entry in another collection · chain A against A, TM-score 1.00
P08200 · AlphaFold monomer V2.0 prediction for isocitrate dehydrogenase [NADP] (P08200) · a predicted model of the same protein · 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 P08200
Elsewhere: RCSB PDB 4ICD · PDBe 4ICD · UniProt P08200

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