MolNFT v1 · #29960 · protein

Isocitrate dehydrogenase from the hyperthermophile thermotoga maritima

1ZOR: “Isocitrate dehydrogenase from the hyperthermophile thermotoga maritima”. X-ray diffraction, 1 ligand (NA), 10 pockets (best druggability 0.80). MolNFT v1 #29960 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1ZOR
Type: protein
Length: 795 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isocitrate dehydrogenase
EC: 1.1.1.42
UniProt: Q9X0N2
Ligands: NA
Pockets: 10 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Isocitrate dehydrogenase (EC 1.1.1.42)	protein	399	46% helix, 22% strand	Q9X0N2
B	Isocitrate dehydrogenase (EC 1.1.1.42)	protein	396	47% helix, 20% strand	Q9X0N2

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	110	0.80	0.99	18	empty
2	165	0.58	0.82	25	empty
3	334	0.58	0.76	42	empty
4	159	0.56	0.81	26	empty
5	274	0.56	0.77	42	empty

Interfaces

1 interface between chains.

A–B · 3442 Å² buried · 55 hydrogen bonds · protein-protein

Compared structures

1ZOR · Isocitrate dehydrogenase from the hyperthermophile Thermotoga maritima · 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 Q9X0N2
Elsewhere: RCSB PDB 1ZOR · PDBe 1ZOR · UniProt Q9X0N2

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