MolNFT v1 · #85847 · protein

Dpidh-NADP. the complex structures of isocitrate dehydrogenase from clostridium thermocellum and desulfotalea psychrophila, support a new active site locking mechanism

4AOV · Isocitrate dehydrogenase [NADP]: “Dpidh-NADP. the complex structures of isocitrate dehydrogenase from clostridium thermocellum and desulfotalea…”. X-ray diffraction, 3 ligands (NAP, ICT, MG), 2 pockets (best druggability 0.55).…

PDB: 4AOV
Type: protein
Length: 401 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isocitrate dehydrogenase [NADP]
EC: 1.1.1.42
UniProt: Q6AQ66
Ligands: NAP, ICT, MG
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Isocitrate dehydrogenase [NADP] (EC 1.1.1.42)	protein	401	44% helix, 24% strand	Q6AQ66

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
ICT · Isocitric acid · ligand · chains A
MG · Magnesium ion · metal · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	298	0.55	0.76	40	NAP, ICT, MG
2	239	0.50	0.75	33	empty

Compared structures

4AOV · DpIDH-NADP. The complex structures of Isocitrate dehydrogenase from Clostridium… · 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 Q6AQ66
Elsewhere: RCSB PDB 4AOV · PDBe 4AOV · UniProt Q6AQ66

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