MolNFT v1 · #190602 · protein
Crystal structure of the catalytic domain of inosine monophosphate dehydrogenase (impdh) from methanocaldococcus jannaschii
7XLO · Inosine-5'-monophosphate dehydrogenase: “Crystal structure of the catalytic domain of inosine monophosphate dehydrogenase (impdh) from…”. X-ray diffraction, 5 pockets (best druggability 0.73). MolNFT v1 #190602 on GenesisL1: 3D…
- PDB
- 7XLO
- Type
- protein
- Length
- 650 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inosine-5'-monophosphate dehydrogenase
- EC
- 1.1.1.205
- UniProt
- Q59011
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 326 | 36% helix, 21% strand | Q59011 |
| B | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 324 | 35% helix, 20% strand | Q59011 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 872 | 0.73 | 0.77 | 90 | empty |
| 2 | 348 | 0.72 | 0.84 | 39 | empty |
| 3 | 394 | 0.68 | 0.81 | 44 | empty |
| 4 | 110 | 0.37 | 0.74 | 19 | empty |
| 5 | 95 | 0.36 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 204 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 7XLO · Crystal Structure of the Catalytic Domain of Inosine Monophosphate Dehydrogenase (IMPDH)… · the same entry in another collection · chain A against A, TM-score 1.00
- Q59011 · AlphaFold monomer V2.0 prediction for inosine-5'-monophosphate dehydrogenase (Q59011) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q59011
- Elsewhere: RCSB PDB 7XLO · PDBe 7XLO · UniProt Q59011
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