Research workbench
Structure of monomeric NADP isocitrate dehydrogenase
Analyse Structure of monomeric NADP isocitrate dehydrogenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B0T
- Type
- protein
- Length
- 735 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
- P50216
- Ligands
- MG
- Pockets
- 10 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADP isocitrate dehydrogenase (EC 1.1.1.42) | protein | 735 | 48% helix, 17% strand | P50216 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.79 | 0.98 | 22 | empty |
| 2 | 312 | 0.58 | 0.77 | 41 | empty |
| 3 | 196 | 0.57 | 0.80 | 36 | empty |
| 4 | 152 | 0.57 | 0.82 | 22 | empty |
| 5 | 111 | 0.40 | 0.76 | 18 | empty |
Compared structures
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 P50216
- Elsewhere: RCSB PDB 2B0T · PDBe 2B0T · UniProt P50216
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