Research workbench

3D structure of E. COLI isocitrate dehydrogenase K100M mutant in complex with alpha-ketoglutarate, CALCIUM(II) and adenine nucleotide phosphate

Analyse 3D structure of E. COLI isocitrate dehydrogenase K100M mutant in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AJC
Type: protein
Length: 415 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NADP isocitrate dehydrogenase
EC: 1.1.1.42
UniProt: Q1RD16
Ligands: A2P, AKG, CA, SO4
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NADP isocitrate dehydrogenase (EC 1.1.1.42)	protein	415	42% helix, 18% strand	Q1RD16

Ligands and binding sites

A2P · Adenosine-2'-5'-diphosphate · ligand · chains A
AKG · 2-oxoglutaric acid · ligand · chains A
CA · Calcium ion · metal · chains A
SO4 · Sulfate ion · ion · 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	503	0.64	0.77	64	AKG, CA
2	114	0.40	0.75	20	A2P

Compared structures

4AJC · 3D structure of E. coli Isocitrate Dehydrogenase K100M mutant in complex with… · the same entry in another collection · 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 Q1RD16
Elsewhere: RCSB PDB 4AJC · PDBe 4AJC · UniProt Q1RD16

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.